SitesBLAST

3tcyA Crystallographic structure of phenylalanine hydroxylase from chromobacterium violaceum (cpah) bound to phenylalanine in a site distal to the active site (see paper)
64% identity, 91% coverage: 14:282/296 of query aligns to 11:277/277 of 3tcyA

query
sites
3tcyA

H

N

A

V

G

G

L

L

E

S

T

H

R

D

A

A

-

N

D

D

F

F

T

T

I

L

D

P

Q

Q

P

P

T

L

E

D

R

R

Y

Y

G

S

A

A

V

E

D

D

H

H

A

A

V

T

W

W

Q

A

Q

T

L

L

Y

Y

A

Q

R

R

Q

Q

T

C

A

K

L

L

K

P

G

G

R

R

V

A

C

C

D

D

E

E

F

F

L

L

A

E

G

G

I

L

D

E

T

R

I

L

G

E

M

V

P

D

P

A

D

D

R

R

V

V

P

P

S

D

F

F

D

N

E

K

I

L

N

N

A

E

K

K

L

L

A

M

P

A

A

A

T

T

G

G

W

W

E

K

I

I

V

V

A

A

V

V

P

P

G

G

L

L

V

I

P

P

D

D

Q

D

V

V

F

F

E

E

H

H

L

L

A

A

N

N

R

R

F

F

P

P

V

V

T

T

W

W

M

L

R

R

R

E

P

P

D

H

Q

Q

L

L

D

D

Y

Y

L

L

Q

Q

E

E

P

P

D

D

C

V

F

F

H
|
H

D

D

L

L

F

F

G

G

H
|
H

V

V

P

P

L

L

I

I

N

N

P

P

V

V

F

F

A

A

D

D

Y

Y

M

L

H

E

A
|
A

Y
|
Y

G

G

R

K

A

G

L

V

A
x
K

A

A

H

K

D

A

A

L

G

G

A

A

L

L

P

P

L

M

L
|
L

A

A

R

R

L

L

Y

Y

W

W

Y

Y

T

T

V

V

E
|
E

F

F

G

G

L

L

I

I

R

N

D

-

A

-

S

T

P

P

N

A

G

G

V

M

K

R

I

I

Y

Y

G

G

A

A

G

G

I

I

V

L

S
|
S

S

S

K

K

G

S

E

E

T

S

L

I

Y

Y

S

C

Q

L

Q

D

S

S

A

A

A

S

P

P

N

N

R

R

L

V

G

G

F

F

G

D

L

L

E

M

R

R

V

I

M

M

R

N

T

T

R

R

Y

Y

R

R

I

I

D

D

T

T

F

F

Q

Q

K

K

T

T

Y

Y

F

F

V

V

I

I

D

D

D

S

F

F

A

K

Q

Q

L

L

F

F

K

D

V

A

A
x
T

Q

A

T
x
P

D
|
D

F
|
F

A

A

P

P

L

L

L

Y

A

L

K

Q

L

L

V

A

A

D

E

A

P

Q

A

P

L

W

A

G

A

A

G

G

D

D

V

I

L

A

E

P

H

D

D

D

R

L

V

V

I

L

active site: H132 (= H134), H137 (= H139), E178 (= E180), S197 (= S202)
binding cobalt (ii) ion: H132 (= H134), H137 (= H139), E178 (= E180)
binding phenylalanine: A152 (= A154), Y153 (= Y155), K159 (≠ A161), L169 (= L171), T248 (≠ A253), P250 (≠ T255), D251 (= D256), F252 (= F257)

4etlA Crystallographic structure of phenylalanine hydroxylase from chromobacterium violaceum f258a mutation (see paper)
63% identity, 91% coverage: 14:282/296 of query aligns to 11:277/277 of 4etlA

query
sites
4etlA

H

N

A

V

G

G

L

L

E

S

T

H

R

D

A

A

-

N

D

D

F

F

T

T

I

L

D

P

Q

Q

P

P

T

L

E

D

R

R

Y

Y

G

S

A

A

V

E

D

D

H

H

A

A

V

T

W

W

Q

A

Q

T

L

L

Y

Y

A

Q

R

R

Q

Q

T

C

A

K

L

L

K

P

G

G

R

R

V

A

C

C

D

D

E

E

F

F

L

L

A

E

G

G

I

L

D

E

T

R

I

L

G

E

M

V

P

D

P

A

D

D

R

R

V

V

P

P

S

D

F

F

D

N

E

K

I

L

N

N

A

E

K

K

L

L

A

M

P

A

A

A

T

T

G

G

W

W

E

K

I

I

V

V

A

A

V

V

P

P

G

G

L

L

V

I

P

P

D

D

Q

D

V

V

F

F

E

E

H

H

L

L

A

A

N

N

R

R

F

F

P

P

V

V

T

T

W

W

M

L

R

R

R

E

P

P

D

H

Q

Q

L

L

D

D

Y

Y

L

L

Q

Q

E

E

P

P

D

D

C

V

F

F

H
|
H

D

D

L

L

F

F

G

G

H
|
H

V

V

P

P

L

L

I

I

N

N

P

P

V

V

F

F

A

A

D

D

Y

Y

M

L

H

E

A

A

Y

Y

G

G

R

K

A

G

L

V

A

K

A

A

H

K

D

A

A

L

G

G

A

A

L

L

P

P

L

M

L

L

A

A

R

R

L

L

Y

Y

W

W

Y

Y

T

T

V

V

E
|
E

F

F

G

G

L

L

I

I

R

N

D

-

A

-

S

T

P

P

N

A

G

G

V

M

K

R

I

I

Y

Y

G

G

A

A

G

G

I

I

V

L

S
|
S

S

S

K

K

G

S

E

E

T

S

L

I

Y

Y

S

C

Q

L

Q

D

S

S

A

A

A

S

P

P

N

N

R

R

L

V

G

G

F

F

G

D

L

L

E

M

R

R

V

I

M

M

R

N

T

T

R

R

Y

Y

R

R

I

I

D

D

T

T

F

F

Q

Q

K

K

T

T

Y

Y

F

F

V

V

I

I

D

D

D

S

F

F

A

K

Q

Q

L

L

F

F

K

D

V

A

A

T

Q

A

T

P

D

D

F

A

A

A

P

P

L

L

L

Y

A

L

K

Q

L

L

V

A

A

D

E

A

P

Q

A

P

L

W

A

G

A

A

G

G

D

D

V

I

L

A

E

P

H

D

D

D

R

L

V

V

I

L

active site: H132 (= H134), H137 (= H139), E178 (= E180), S197 (= S202)
binding cobalt (ii) ion: H132 (= H134), H137 (= H139), E178 (= E180)

1ltzA Crystal structure of chromobacterium violaceum phenylalanine hydroxylase, structure has bound iron (iii) and oxidized cofactor 7, 8-dihydrobiopterin (see paper)
64% identity, 91% coverage: 14:282/296 of query aligns to 11:274/274 of 1ltzA

query
sites
1ltzA

H

N

A

V

G

G

L

L

E

S

T

H

R

D

A

A

-

N

D

D

F

F

T

T

I

L

D

P

Q

Q

P

P

T

L

E

D

R

R

Y

Y

G

S

A

A

V

E

D

D

H

H

A

A

V

T

W

W

Q

A

Q

T

L

L

Y

Y

A

Q

R

R

Q

Q

T

C

A

K

L

L

K

P

G

G

R

R

V

A

C

C

D

D

E

E

F

F

L

L

A

E

G

G

I

L

D

E

T

R

I

L

G

E

M

V

P

D

P

A

D

D

R

R

V

V

P

P

S

D

F

F

D

N

E

K

I

L

N

N

A

E

K

K

L

L

A

M

P

A

A

A

T

T

G

G

W

W

E

K

I

I

V

V

A

A

V

V

P

P

G

G

L

L

V
x
I

P

P

D
|
D

Q

D

V

V

F
|
F

F

F

E

E

H

H

L

L

A

A

N

N

R

R

F

F

P

P

V

V

T

T

W

W

M

L

R

R

R

E

P

P

D

H

Q

Q

L

L

D

D

Y

Y

L

L

Q

Q

E

E

P

P

D

D

C

V

F

F

H
|
H

D

D

L

L

F

F

G

G

H
|
H

V

V

P

P

L

L

I

I

N

N

P

P

V

V

F

F

A

A

D

D

Y

Y

M

L

H

E

A

A

Y

Y

G

G

R

K

A

G

L

V

A

K

A

A

H

K

D

A

A

L

G

G

A

A

L

L

P

P

L

M

L

L

A

A

R

R

L

L

Y
|
Y

W

W

Y

Y

T

T

V

V

E
|
E

F

F

G

G

L

L

I

I

R

N

D

-

A

-

S

T

P

P

N

A

G

G

V

M

K

R

I

I

Y

Y

G

G

A

A

G

G

I

I

V

L

S
|
S

S

S

K

K

G

S

E

E

T

S

L

I

Y

Y

S

C

Q

L

Q

D

S

S

A

A

A

S

P

P

N

N

R

R

L

V

G

G

F

F

G

D

L

L

E

M

R

R

V

I

M

M

R

N

T

T

R

R

Y

Y

R

R

I

I

D

D

T

T

F

F

Q

Q

K

K

T

T

Y

Y

F

F

V

V

I

I

D

D

D

S

F

F

A

K

Q

Q

L

L

F

F

K

-

V

-

A

-

Q

D

T

A

D

D

F

F

A

A

P

P

L

L

L

Y

A

L

K

Q

L

L

V

A

A

D

E

A

P

Q

A

P

L

W

A

G

A

A

G

G

D

D

V

I

L

A

E

P

H

D

D

D

R

L

V

V

I

L

active site: H132 (= H134), H137 (= H139), E178 (= E180), S197 (= S202)
binding fe (iii) ion: H132 (= H134), H137 (= H139), E178 (= E180)
binding 7,8-dihydrobiopterin: I96 (≠ V98), D98 (= D100), F101 (= F103), Y173 (= Y175)

2v27B Structure of the cold active phenylalanine hydroxylase from colwellia psychrerythraea 34h (see paper)
41% identity, 77% coverage: 36:263/296 of query aligns to 21:247/272 of 2v27B

query
sites
2v27B

D

E

H

N

A

L

V

I

W

W

Q

Q

Q

E

L

L

Y

F

A

T

R

R

Q

Q

T

I

A

A

L

C

L

I

K

K

G

D

R

K

V

A

C

C

D

D

E

E

F

Y

L

H

A

E

G

G

I

L

D

A

T

K

I

L

G

N

M

L

P

P

P

T

D

D

R

R

V

I

P

P

S

Q

F

L

D

D

E

E

I

V

N

S

A

K

K

V

L

L

A

K

P

V

A

S

T

T

G

G

W

W

E

E

I

C

V

Y

A

P

V

V

P

P

G

A

L

L

V

I

P

G

D

F

Q

G

V

E

F

F

E

R

H

L

L

L

A

S

N

E

R

K

F

F

P

P

V

V

T

A

W

T

W

F

M

I

R

R

R

S

P

R

D

E

Q

E

L

M

D

D

Y

Y

L

L

Q

Q

E

E

P

P

D

D

C

I

F

F

H
|
H

D

E

L

I

F

F

G

G

H
|
H

V

C

P

P

L

L

I

T

N

N

P

S

V

S

F

F

A

A

D

N

Y

Y

M

T

H

E

A

A

Y

Y

G

G

R

K

A

M

A

G

L

L

A

N

A

A

H

T

D

K

A

E

G

Q

A

R

L

V

P

-

L

F

L

L

A

A

R

R

L

L

Y

Y

W

W

Y

F

T

T

V

I

E
|
E

F

F

G

G

L

L

I

L

R

-

D

-

A

-

A

D

S

T

P

P

N

K

G

G

V

L

K

R

I

I

Y

Y

G

G

A

G

G

G

I

V

V

L

S
|
S

S

S

K

P

G

G

E

E

T

T

L

D

Y

Y

S

A

Q

M

Q

N

S

N

A

T

A

D

P

V

N

D

R

R

L

K

G

P

F

F

G

D

L

I

E

L

R

D

V

V

M

L

R

R

T

T

R

P

Y

Y

R

R

I

I

D

D

T

I

F

M

Q

Q

K

P

T

I

Y

Y

F

Y

V

M

-

L

-

T

-

K

I

V

D

S

D

D

F

L

A

D

Q

E

L

I

F

R

K

K

V

F

A

E

Q

V

T

D

D

D

F

I

A

M

P

E

L

L

L

V

A

A

K

Q

active site: H119 (= H134), H124 (= H139), E164 (= E180), S183 (= S202)
binding fe (iii) ion: H119 (= H134), H124 (= H139), E164 (= E180)

5jk5A Phenylalanine hydroxylase from dictyostelium - bh2 complex
36% identity, 75% coverage: 28:248/296 of query aligns to 149:368/400 of 5jk5A

query
sites
5jk5A

P

P

T

R

E

I

R

D

Y

Y

G

T

A

E

V

E

D

E

H

I

A

K

V

T

W

W

Q

G

Q

V

L

V

Y

Y

A

N

R

R

Q

L

T

K

A

E

L

L

L

F

K

P

G

T

R

N

V

A

C

C

D

H

E

Q

-

H

-

A

-

Y

-

I

F

F

L

P

A

L

G

L

I

E

D

Q

T

N

I

C

G

G

M

Y

P

S

P

P

D

D

R

N

V

I

P

P

S

Q

F

L

D

Q

E

D

I

I

N

S

A

N

K

F

L

L

A

Q

P

E

A

C

T
|
T

G

G

W

W

E

R

I

I

V

R

A

P

V

V

P

Q

G
|
G

L
|
L

V
x
L

P

S

D

A

Q

R

V

D

F
|
F

F
x
L

E

N

H

G

L

L

A

A

N

F

R

R

R

V

F

F

P

H

V

A

T

T

W

Q

W

Y

M

I

R

R

R

H

P

P

D

S

Q

V

L

P

D

L

Y

Y

L

T

Q

P

E

E

P

P

D

D

C

C

F

C

H
|
H

D

E

L

L

F

L

G

G

H
|
H

V

V

P

P

L

L

I

A

N

D

P
|
P

V

D

F

F

A

A

D
|
D

Y

F

M

S

H

Q

A

E

Y

I

G

G

R

L

A

A

A

S

L

I

A

G

A

A

H

S

D

D

A

E

G

D

A

-

L

I

P

Q

L

L

A
x
S

R

T

L

C

Y
|
Y

W

W

Y

F

T

T

V

V

E
|
E

F

F

G

G

L

L

I

C

R

K

D

E

A

G

A

-

S

-

P

-

N

D

G

T

V

I

K

R

I

A

Y

Y

G

G

A

A

G

G

I

I

V

L

S
|
S

S

S

K

T

G

G

E

E

T

M

L

E

Y

H

S

F

Q

L

Q

T

S

D

A

K

A

A

P

-

N

K

R

K

L

L

G

P

F

F

G

N

L

P

E

F

R

D

V

A

M

C

R

N

T

T

R

E

Y

Y

R

P

I

I

D

T

T

T

F

F

Q

Q

K

P

T

L

Y

Y

F

Y

V

V

I

A

D

E

D

S

F

F

A

Q

Q

K

active site: H259 (= H134), H264 (= H139), E304 (= E180), S323 (= S202)
binding fe (iii) ion: H259 (= H134), H264 (= H139), E304 (= E180)
binding 7,8-dihydrobiopterin: G221 (= G96), L222 (= L97), L223 (≠ V98), F228 (= F103), L229 (≠ F104), S296 (≠ A172), Y299 (= Y175)
binding piperazine-n,n'-bis(2-ethanesulfonic acid): T212 (= T87), P271 (= P146), D275 (= D150)

Sites not aligning to the query:

binding piperazine-n,n'-bis(2-ethanesulfonic acid): 374

5jk8A Phenylalanine hydroxylase from dictyostelium - bh2, norleucine complex
36% identity, 75% coverage: 28:248/296 of query aligns to 140:359/390 of 5jk8A

query
sites
5jk8A

P

P

T

R

E

I

R

D

Y

Y

G

T

A

E

V

E

D

E

H

I

A

K

V

T

W

W

Q

G

Q

V

L

V

Y

Y

A

N

R

R

Q

L

T

K

A

E

L

L

L

F

K

P

G

T

R

N

V

A

C

C

D

H

E

Q

-

H

-

A

-

Y

-

I

F

F

L

P

A

L

G

L

I

E

D

Q

T

N

I

C

G

G

M

Y

P

S

P

P

D

D

R

N

V

I

P

P

S

Q

F

L

D

Q

E

D

I

I

N

S

A

N

K

F

L

L

A

Q

P

E

A

C

T
|
T

G

G

W

W

E

R

I

I

V

R

A

P

V

V

P

Q

G

G

L

L

V
x
L

P

S

D
x
A

Q

R

V

D

F
|
F

F

L

E

N

H

G

L

L

A

A

N

F

R
|
R

R

V

F

F

P

H

V

A

T

T

W

Q

W

Y

M

I

R

R

R

H

P

P

D

S

Q

V

L

P

D

L

Y
|
Y

L
x
T

Q

P

E

E

P

P

D

D

C

C

F

C

H
|
H

D

E

L

L

F

L

G

G

H
|
H

V

V

P

P

L

L

I

A

N

D

P

P

V

D

F

F

A

A

D
|
D

Y

F

M

S

H

Q

A

E

Y

I

G

G

R

L

A

A

A

S

L

I

A

G

A

A

H

S

D

D

A

E

G

D

A

-

L

I

P

Q

L

L

A
x
S

R

T

L

C

Y
|
Y

W

W

Y

F

T

T

V

V

E
|
E

F

F

G

G

L

L

I

C

R

K

D

E

A

G

A

-

S

-

P

-

N

D

G

T

V

I

K

R

I

A

Y

Y

G

G

A

A

G

G

I

I

V

L

S
|
S

K

T

G

G

E

E

T

M

L

E

Y

H

S

F

Q

L

Q

T

S

D

A

K

A

A

P

-

N

K

R

K

L

L

G

P

F

F

G

N

L

P

E

F

R

D

V

A

M

C

R

N

T

T

R

E

Y

Y

R

P

I

I

D

T

T

T

F

F

Q

Q

K

P

T

L

Y

Y

F

Y

V

V

I

A

D

E

D

S

F

F

A

Q

Q

K

active site: H250 (= H134), H255 (= H139), E295 (= E180), S314 (= S202)
binding fe (iii) ion: H250 (= H134), H255 (= H139), E295 (= E180)
binding 7,8-dihydrobiopterin: L214 (≠ V98), A216 (≠ D100), F219 (= F103), S287 (≠ A172), Y290 (= Y175)
binding norleucine: Y242 (= Y126), T243 (≠ L127), H250 (= H134), S314 (= S202), S315 (= S203)
binding piperazine-n,n'-bis(2-ethanesulfonic acid): T203 (= T87), R226 (= R110), D266 (= D150)

Sites not aligning to the query:

binding piperazine-n,n'-bis(2-ethanesulfonic acid): 44, 365, 382

6zn2A Partial structure of tyrosine hydroxylase in complex with dopamine showing the catalytic domain and an alpha-helix from the regulatory domain involved in dopamine binding. (see paper)
34% identity, 89% coverage: 28:289/296 of query aligns to 58:319/335 of 6zn2A

query
sites
6zn2A

P

P

T

R

E

V

R

E

Y

Y

G

T

A

A

V

E

D

E

H

I

A

A

V

T

W

W

Q

K

Q

E

L

V

Y

Y

A

T

R

T

Q

L

T

K

A

G

L

L

L

Y

K

A

G

T

R

H

V

A

C

C

D

G

E

E

F

H

L

L

A

E

G

A

I

F

D

A

T

L

I

L

-

E

-

R

-

F

-

S

G

G

M

Y

P

R

P

E

D

D

R

N

V

I

P

P

S

Q

F

L

D

E

E

D

I

V

N

S

A

R

K

F

L

L

A

K

P

E

A

R

T

T

G

G

W

F

E

Q

I

L

V

R

A

P

V

V

P

A

G

G

L

L

V

L

P

S

D
x
A

Q

R

V

D

F

F

F

L

E

A

H

S

L

L

A

A

N

F

R

R

R

V

F

F

P

Q

V

C

T

T

W

Q

W

Y

M

I

R

R

R

H

P

A

D

S

Q

S

L

P

D

M

Y

H

L

S

Q

P

E

E

P
|
P

D

D

C

C

F

C

H
|
H

D

E

L

L

F

L

G

G

H
|
H

V

V

P

P

L

M

L

L

I

A

N

D

P

R

V

T

F

F

A

A

D

Q

Y

F

M

S

H

Q

A

D

Y

I

G

G

R

L

A

A

A

S

L

L

A

G

A

A

H

S

D

D

A

E

G

-

A

E

L

I

P
x
E

L

K

L

L

A
x
S

R

T

L

L

Y
|
Y

W
|
W

Y

F

T

T

V

V

E
|
E

F

F

G

G

L

L

I

C

R

K

D

Q

A

-

S

-

P

-

N

N

G

G

-

E

V

V

K

K

I

A

Y

Y

G

G

A

A

G

G

I

L

V

L

S

S

K

Y

G

G

E

E

T

L

L

L

Y

H

S

C

Q

-

Q

L

S

S

A

E

P

P

N

E

R

I

L

R

G

A

F

F

G

D

L

P

E

E

R

A

V

A

M

A

R

V

T

Q

R

P

Y
|
Y

R

Q

I

D

D

Q

T

T

F

Y

Q

Q

K

S

T

V

Y

Y

F

F

V

V

I

S

D

E

D

S

F

F

A

S

-

D

-

A

-

K

-

D

Q

K

L

L

F

R

K

S

V

Y

A

A

Q

S

T

R

D

I

F

Q

A

R

P

P

L

F

L

S

A

V

K

K

L

F

V

-

A

-

E

D

P

P

A

Y

L

T

A

L

A

A

G

I

D

D

V

V

L

L

E

D

H

S

D

P

R

Q

V

A

I

V

T

R

R

R

G

-

S

S

Q

L

E

E

G

G

binding fe (iii) ion: H168 (= H134), H173 (= H139), E213 (= E180)
binding l-dopamine: P164 (= P130), H173 (= H139), E213 (= E180)
binding : A134 (≠ D100), E202 (≠ P169), S205 (≠ A172), Y208 (= Y175), W209 (= W176), Y260 (= Y231)

2xsnA Crystal structure of human tyrosine hydroxylase catalytic domain
34% identity, 89% coverage: 28:289/296 of query aligns to 59:320/335 of 2xsnA

query
sites
2xsnA

P

P

T

R

E

V

R

E

Y

Y

G

T

A

A

V

E

D

E

H

I

A

A

V

T

W

W

Q

K

Q

E

L

V

Y

Y

A

T

R

T

Q

L

T

K

A

G

L

L

L

Y

K

A

G

T

R

H

V

A

C

C

D

G

E

E

F

H

L

L

A

E

G

A

I

F

D

A

T

L

I

L

-

E

-

R

-

F

-

S

G

G

M

Y

P

R

P

E

D

D

R

N

V

I

P

P

S

Q

F

L

D

E

E

D

I

V

N

S

A

R

K

F

L

L

A

K

P

E

A

R

T

T

G

G

W

F

E

Q

I

L

V

R

A

P

V

V

P

A

G

G

L

L

V

L

P

S

D

A

Q

R

V

D

F

F

F

L

E

A

H

S

L

L

A

A

N

F

R

R

R

V

F

F

P

Q

V

C

T

T

W

Q

W

Y

M

I

R

R

R

H

P

A

D

S

Q

S

L

P

D

M

Y

H

L

S

Q

P

E

E

P

P

D

D

C

C

F

C

H
|
H

D

E

L

L

F

L

G

G

H
|
H

V

V

P

P

L

M

L

L

I

A

N

D

P

R

V

T

F

F

A

A

D

Q

Y

F

M

S

H

Q

A

D

Y

I

G

G

R

L

A

A

A

S

L

L

A

G

A

A

H

S

D

D

A

E

G

-

A

E

L

I

P

E

L

K

L

L

A

S

R

T

L

L

Y

Y

W

W

Y

F

T

T

V

V

E
|
E

F

F

G

G

L

L

I

C

R

K

D

Q

A

-

S

-

P

-

N

N

G

G

-

E

V

V

K

K

I

A

Y

Y

G

G

A

A

G

G

I

L

V

L

S
|
S

S

S

K

Y

G

G

E

E

T

L

L

L

Y

H

S

C

Q

-

Q

L

S

S

A

E

P

P

N

E

R

I

L

R

G

A

F

F

G

D

L

P

E

E

R

A

V

A

M

A

R

V

T

Q

R

P

Y

Y

R

Q

I

D

D

Q

T

T

F

Y

Q

Q

K

S

T

V

Y

Y

F

F

V

V

I

S

D

E

D

S

F

F

A

S

-

D

-

A

-

K

-

D

Q

K

L

L

F

R

K

S

V

Y

A

A

Q

S

T

R

D

I

F

Q

A

R

P

P

L

F

L

S

A

V

K

K

L

F

V

-

A

-

E

D

P

P

A

Y

L

T

A

L

A

A

G

I

D

D

V

V

L

L

E

D

H

S

D

P

R

Q

V

A

I

V

T

R

R

R

G

-

S

S

Q

L

E

E

G

G

active site: H169 (= H134), H174 (= H139), E214 (= E180), S233 (= S202)
binding zinc ion: H169 (= H134), H174 (= H139), E214 (= E180)

6zvpD Atomic model of the em-based structure of the full-length tyrosine hydroxylase in complex with dopamine (residues 40-497) in which the regulatory domain (residues 40-165) has been included only with the backbone atoms (see paper)
34% identity, 89% coverage: 28:289/296 of query aligns to 181:442/458 of 6zvpD

query
sites
6zvpD

P

P

T

R

E

V

R

E

Y

Y

G

T

A

A

V

E

D

E

H

I

A

A

V

T

W

W

Q

K

Q

E

L

V

Y

Y

A

T

R

T

Q

L

T

K

A

G

L

L

L

Y

K

A

G

T

R

H

V

A

C

C

D

G

E

E

F

H

L

L

A

E

G

A

I

F

D

A

T

L

I

L

-

E

-

R

-

F

-

S

G

G

M

Y

P

R

P

E

D

D

R

N

V

I

P

P

S

Q

F

L

D

E

E

D

I

V

N

S

A

R

K

F

L

L

A

K

P

E

A

R

T

T

G

G

W

F

E

Q

I

L

V

R

A

P

V

V

P

A

G

G

L

L

V

L

P

S

D

A

Q

R

V

D

F

F

F

L

E

A

H

S

L

L

A

A

N

F

R

R

R

V

F

F

P

Q

V

C

T

T

W

Q

W

Y

M

I

R

R

R

H

P

A

D

S

Q

S

L

P

D

M

Y

H

L

S

Q

P

E

E

P
|
P

D

D

C

C

F

C

H
|
H

D

E

L

L

F

L

G

G

H
|
H

V

V

P

P

L

M

L

L

I

A

N

D

P

R

V

T

F

F

A

A

D

Q

Y

F

M

S

H

Q

A

D

Y

I

G

G

R

L

A

A

A

S

L

L

A

G

A

A

H

S

D

D

A

E

G

-

A

E

L

I

P

E

L

K

L

L

A

S

R

T

L

L

Y
|
Y

W

W

Y

F

T

T

V

V

E
|
E

F

F

G

G

L

L

I

C

R

K

D

Q

A

-

S

-

P

-

N

N

G

G

-

E

V

V

K

K

I

A

Y

Y

G

G

A
|
A

G

G

I

L

V

L

S

S

K

Y

G

G

E

E

T

L

L

L

Y

H

S

C

Q

-

Q

L

S

S

A

E

P

P

N

E

R

I

L

R

G

A

F

F

G

D

L

P

E

E

R

A

V

A

M

A

R

V

T

Q

R

P

Y

Y

R

Q

I

D

D

Q

T

T

F

Y

Q

Q

K

S

T

V

Y

Y

F

F

V

V

I

S

D

E

D

S

F

F

A

S

-

D

-

A

-

K

-

D

Q

K

L

L

F

R

K

S

V

Y

A

A

Q

S

T

R

D

I

F

Q

A

R

P

P

L

F

L

S

A

V

K

K

L

F

V

-

A

-

E

D

P

P

A

Y

L

T

A

L

A

A

G

I

D

D

V

V

L

L

E

D

H

S

D

P

R

Q

V

A

I

V

T

R

R

R

G

-

S

S

Q

L

E

E

G

G

binding fe (iii) ion: H291 (= H134), H296 (= H139), E336 (= E180), A351 (= A198)
binding l-dopamine: P287 (= P130), H291 (= H134), H296 (= H139), Y331 (= Y175), E336 (= E180)

Sites not aligning to the query:

binding l-dopamine: 2

P07101 Tyrosine 3-monooxygenase; Tyrosine 3-hydroxylase; TH; EC 1.14.16.2 from Homo sapiens (Human) (see 32 papers)
34% identity, 89% coverage: 28:289/296 of query aligns to 251:512/528 of P07101

query
sites
P07101

P

P

T

R

E

V

R

E

Y

Y

G

T

A

A

V

E

D
x
E

H

I

A

A

V

T

W

W

Q

K

Q

E

L

V

Y

Y

A

T

R

T

Q

L

T

K

A

G

L

L

L

Y

K

A

G
x
T

R

H

V

A

C

C

D

G

E

E

F

H

L

L

A

E

G

A

I

F

D

A

T

L

I

L

-

E

-

R

-

F

-

S

G

G

M

Y

P

R

P

E

D

D

R

N

V

I

P
|
P

S

Q

F

L

D

E

E

D

I

V

N

S

A

R

K
x
F

L

L

A

K

P

E

A

R

T
|
T

G

G

W

F

E

Q

I

L

V
x
R

A

P

V

V

P

A

G

G

L

L

V

L

P

S

D

A

Q
x
R

V

D

F

F

F

L

E

A

H

S

L

L

A

A

N

F

R
|
R

R

V

F

F

P

Q

V

C

T

T

W

Q

W

Y

M

I

R

R

R

H

P

A

D

S

Q

S

L

P

D

M

Y

H

L

S

Q

P

E

E

P

P

D

D

C
|
C

F

C

H

H

D

E

L

L

F

L

G

G

H

H

V

V

P

P

L

M

L

L

I

A

N

D

P

R

V

T

F
|
F

A
|
A

D

Q

Y

F

M

S

H

Q

A

D

Y

I

G

G

R

L

A

A

A

S

L
|
L

A

G

A

A

H

S

D

D

A

E

G

-

A

E

L
x
I

P

E

L

K

L

L

A

S

R
x
T

L

L

Y

Y

W

W

Y

F

T

T

V

V

E

E

F

F

G

G

L

L

I

C

R

K

D
x
Q

A

-

S

-

P

-

N

N

G
|
G

-

E

V

V

K

K

I

A

Y

Y

G

G

A

A

G

G

I

L

V

L

S

S

K

Y

G
|
G

E

E

T

L

L

L

Y

H

S

C

Q

-

Q

L

S

S

A

E

P

P

N

E

R

I

L
x
R

G

A

F

F

G

D

L

P

E

E

R

A

V

A

M

A

R

V

T

Q

R

P

Y

Y

R

Q

I

D

D

Q

T

T

F

Y

Q

Q

K

S

T

V

Y

Y

F

F

V

V

I

S

D

E

D
x
S

F

F

A

S

-

D

-

A

-

K

-

D

Q

K

L

L

F

R

K

S

V

Y

A

A

Q

S

T

R

D

I

F

Q

A

R

P

P

L

F

L

S

A

V

K

K

L

F

V

-

A

-

E

D

P
|
P

A

Y

L
x
T

A

L

A

A

G

I

D
|
D

V
|
V

L

L

E

D

H

S

D

P

R

Q

V

A

I

V

T

R

R

R

G

-

S

S

Q
x
L

E

E

G

G

E259 (≠ D36) to G: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity
T276 (≠ G53) to P: in ARSEGS; parkinsonian symptoms in infancy; no effect on tyrosine 3-monooxygenase activity; dbSNP:rs28934581
P301 (= P74) to A: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity
F309 (≠ K82) to S: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity
T314 (= T87) to M: in ARSEGS; parkinsonian symptoms in infancy; loss of about 80% of tyrosine 3-monooxygenase activity; dbSNP:rs121917764
R319 (≠ V92) to P: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity
R328 (≠ Q101) to W: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity; dbSNP:rs1428589694
R337 (= R110) to H: in ARSEGS; parkinsonian symptoms in infancy; no effect on tyrosine 3-monooxygenase activity; dbSNP:rs28934580
C359 (= C132) to F: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; dbSNP:rs121917765
F375 (= F148) to L: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; shifted substrate specificity from tyrosine to phenylalanine and Dopa; dbSNP:rs763198914
A376 (= A149) to V: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity
L387 (= L160) to M: in ARSEGS; no effect on tyrosine 3-monooxygenase activity
I394 (≠ L168) to T: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity
T399 (≠ R173) to M: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; dbSNP:rs1057520384
Q412 (≠ D186) to K: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; reduced affinity for L-tyrosine; dbSNP:rs121917762
G414 (= G192) to R: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; dbSNP:rs370962049
G428 (= G205) to R: in ARSEGS; phenotype with prominent levodopa-responsive myoconus-dystonia (M-D); dbSNP:rs1264884607
R441 (≠ L219) to P: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity; dbSNP:rs367874223
S467 (≠ D245) to G: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity
P492 (= P268) to L: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity; dbSNP:rs767635052
T494 (≠ L270) to M: in ARSEGS; parkinsonian symptoms in infancy; no effect on tyrosine 3-monooxygenase activity; dbSNP:rs45471299
D498 (= D274) to G: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; dbSNP:rs771351747
V499 (= V275) to M: in dbSNP:rs1800033
L510 (≠ Q287) to Q: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity

Sites not aligning to the query:

19 modified: Phosphoserine; by CaMK2; S → C: found in a patient with ARSEGS; uncertain significance; dbSNP:rs766704202
62 modified: Phosphoserine; S→A: Affects subcellular localization. Accumulates mainly in the soma of the neuroblastoma cells.; S→E: Does not affect subcellular localization. Distributed throughout the soma and neurites.
71 modified: Phosphoserine; by CaMK2 and PKA; S→E: Suppresses feedback inhibition induced by dopamine. Suppresses feedback inhibition induced by dopamine; when associated with A-207.
112 V → M: in dbSNP:rs6356
207 C → Y: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; C→A: Suppresses the decrease in tyrosine 3-monooxygenase activity induced by NEM modification. Suppresses feedback inhibition induced by dopamine; when associated with E-71.
227 D → G: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity
233 R → H: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; shifted substrate specificity from tyrosine to phenylalanine and Dopa; dbSNP:rs80338892
236 L → P: in ARSEGS; severe parkinsonian symptoms in early infancy; strongly reduced stability and tyrosine 3-monooxygenase activity; rare mutation; dbSNP:rs121917763
241 A → T: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; dbSNP:rs1260455415
246 H → Y: in ARSEGS; loss of about 40% of tyrosine 3-monooxygenase activity
247 G → S: in ARSEGS; loss of about 50% of tyrosine 3-monooxygenase activity; shifted substrate specificity from tyrosine to phenylalanine and Dopa; dbSNP:rs762304556

P04177 Tyrosine 3-monooxygenase; Tyrosine 3-hydroxylase; TH; EC 1.14.16.2 from Rattus norvegicus (Rat) (see 7 papers)
33% identity, 87% coverage: 28:285/296 of query aligns to 221:479/498 of P04177

query
sites
P04177

P

P

T

H

E

V

R

E

Y

Y

G

T

A

A

V

E

D

E

H

I

A

A

V

T

W

W

Q

K

Q

E

L

V

Y

Y

A

V

R

T

Q

L

T

K

A

G

L

L

L

Y

K

A

G

T

R

H

V

A

C

C

D

R

E

E

F

H

L

L

A

E

G

G

I

F

D

Q

T

L

I

L

-

E

-

R

-

Y

-

C

G

G

M

Y

P

R

P

E

D

D

R

S

V

I

P

P

S

Q

F

L

D

E

E

D

I

V

N

S

A

R

K

F

L

L

A

K

P

E

A

R

T

T

G

G

W

F

E

Q

I

L

V

R

A

P

V

V

P

A

G

G

L

L

V

L

P

S

D

A

Q

R

V

D

F

F

F

L

E

A

H

S

L

L

A

A

N

F

R

R

R

V

F

F

P
x
Q

V

C

T

T

W

Q

W

Y

M

I

R

R

R

H

P

A

D

S

Q

S

L

P

D

M

Y
x
H

L

S

Q

P

E

E

P

P

D

D

C

C

F

C

H
|
H

D

E

L

L

F

L

G

G

H
|
H

V

V

P

P

L

M

L

L

I

A

N

D

P

R

V

T

F

F

A

A

D

Q

Y

F

M

S

H

Q

A

D

Y

I

G

G

R

L

A

A

A

S

L

L

A

G

A

A

H

S

D

D

A

E

G

-

A

E

L

I

P

E

L

K

L

L

A

S

R

T

L

V

Y

Y

W
|
W

Y

F

T

T

V

V

E
|
E

F

F

G

G

L

L

I

C

R

K

D

Q

A

-

S

-

P

-

N

N

G

G

-

E

V

L

K

K

I

A

Y

Y

G

G

A

A

G

G

I

L

V

L

S

S

K

Y

G

G

E

E

T

L

L

L

Y

H

S

S

Q

-

Q

L

S

S

A

E

P

P

N

E

R

V

L

R

G

A

F

F

G

D

L

P

E

D

R

T

V

A

M

A

R

V

T

Q

R

P

Y

Y

R

Q

I
x
D

D

Q

T

T

F

Y

Q

Q

K

P

T

V

Y

Y

F

F

V

V

I

S

D

E

D

S

F

F

A

N

-

D

-

A

-

K

-

D

Q

K

L

L

F

R

K

N

V

Y

A

A

Q

S

T

R

D

I

F

Q

A

R

P

P

L

F

L

S

A

V

K

K

L

F

V

-

A

-

E

D

P

P

A

Y

L

T

A

L

A

A

G

I

D

D

V

V

L

L

E

D

H

S

D

P

R

H

V

T

I

I

T

Q

R

R

G

S

Q310 (≠ P113) mutation to H: Does not affect Vmax for phenylalanine. Increases KM for phenylalanine.
H323 (≠ Y126) mutation to Y: Does not affect Vmax for phenylalaninet. Increases KM for phenylalanine.
H331 (= H134) binding
H336 (= H139) binding
W372 (= W176) mutation to F: Does not affect substrate specificity.
E376 (= E180) binding
D425 (≠ I233) Important for substrate specificity; mutation to V: Shifts substrate specificity from tyrosine to phenylalanine.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
19 modified: Phosphoserine; by CaMK2
31 modified: Phosphoserine
40 modified: Phosphoserine; by CaMK2 and PKA

2tohA Tyrosine hydroxylase catalytic and tetramerization domains from rat (see paper)
33% identity, 89% coverage: 28:289/296 of query aligns to 59:320/336 of 2tohA

query
sites
2tohA

P

P

T

H

E

V

R

E

Y

Y

G

T

A

A

V

E

D

E

H

I

A

A

V

T

W

W

Q

K

Q

E

L

V

Y

Y

A

V

R

T

Q

L

T

K

A

G

L

L

L

Y

K

A

G

T

R

H

V

A

C

C

D

R

E

E

F

H

L

L

A

E

G

G

I

F

D

Q

T

L

I

L

-

E

-

R

-

Y

-

C

G

G

M

Y

P

R

P

E

D

D

R

S

V

I

P

P

S

Q

F

L

D

E

E

D

I

V

N

S

A

R

K

F

L

L

A

K

P

E

A

R

T

T

G

G

W

F

E

Q

I

L

V

R

A

P

V
|
V

P

A

G

G

L
|
L

V
x
L

P

S

D

A

Q

R

V

D

F
x
Y

F

L

E

A

H

S

L

L

A

A

N

F

R

R

R

V

F

F

P

Q

V

C

T

T

W

Q

W

Y

M

I

R

R

R

H

P

A

D

S

Q

S

L

P

D

M

Y

H

L

S

Q

P

E

E

P
|
P

D

D

C

C

F

C

H
|
H

D
x
E

L

L

F

L

G

G

H
|
H

V

V

P

P

L

M

L

L

I

A

N

D

P

R

V

T

F

F

A

A

D

Q

Y

F

M

S

H

Q

A

D

Y

I

G

G

R

L

A

A

A

S

L

L

A

G

A

A

H

S

D

D

A

E

G

-

A

E

L

I

P

E

L

K

L

L

A

S

R

T

L

V

Y
|
Y

W

W

Y

F

T

T

V

V

E
|
E

F

F

G

G

L

L

I

C

R

K

D

Q

A

-

S

-

P

-

N

N

G

G

-

E

V

L

K

K

I

A

Y

Y

G

G

A

A

G

G

I

L

V

L

S
|
S

S

S

K

Y

G

G

E

E

T

L

L

L

Y

H

S

S

Q

-

Q

L

S

S

A

E

P

P

N

E

R

V

L

R

G

A

F

F

G

D

L

P

E

D

R

T

V

A

M

A

R

V

T

Q

R

P

Y

Y

R

Q

I

D

D

Q

T

T

F

Y

Q

Q

K

P

T

V

Y

Y

F

F

V

V

I

S

D

E

D

S

F

F

A

N

-

D

-

A

-

K

-

D

Q

K

L

L

F

R

K

N

V

Y

A

A

Q

S

T

R

D

I

F

Q

A

R

P

P

L

F

L

S

A

V

K

K

L

F

V

-

A

-

E

D

P

P

A

Y

L

T

A

L

A

A

G

I

D

D

V

V

L

L

E

D

H

S

D

P

R

H

V

T

I

I

T

Q

R

R

G

-

S

S

Q

L

E

E

G

G

active site: H169 (= H134), H174 (= H139), E214 (= E180), S233 (= S202)
binding fe (iii) ion: H169 (= H134), H174 (= H139), E214 (= E180)
binding 7,8-dihydrobiopterin: V129 (= V94), L132 (= L97), L133 (≠ V98), Y138 (≠ F103), P165 (= P130), E170 (≠ D135), Y209 (= Y175)

P17289 Tyrosine 3-monooxygenase; Tyrosine 3-hydroxylase; TH; EC 1.14.16.2 from Bos taurus (Bovine) (see 2 papers)
34% identity, 74% coverage: 28:247/296 of query aligns to 214:432/491 of P17289

query
sites
P17289

P

P

T

H

E

V

R

E

Y

Y

G

T

A

A

V

E

D

E

H

T

A

A

V

T

W

W

Q

K

Q

E

L

V

Y

Y

A

S

R

T

Q

L

T

R

A

G

L

L

L

Y

K

P

G

T

R

H

V

A

C

C

D

R

E

E

F

H

L

L

A

E

G

A

I

F

D

E

T

L

I

L

-

E

-

R

-

F

-

C

G

G

M

Y

P

R

P

E

D

D

R

R

V

I

P

P

S

Q

F

L

D

E

E

D

I

V

N

S

A

R

K

F

L

L

A

K

P

E

A

R

T

T

G

G

W

F

E

Q

I

L

V

R

A

P

V

A

P

A

G

G

L

L

V

L

P

S

D

A

Q

R

V

D

F

F

F

L

E

A

H

S

L

L

A

A

N

F

R

R

R

V

F

F

P

Q

V

C

T

T

W

Q

W

Y

M

I

R

R

R

H

P

A

D

S

Q

S

L

P

D

M

Y

H

L

S

Q

P

E

E

P

P

D

E

C

C

F

C

H

H

D

E

L

L

F

L

G

G

H

H

V

V

P

P

L

M

L

L

I

A

N

D

P

R

V

T

F

F

A

A

D

Q

Y

F

M

S

H

Q

A

D

Y

I

G

G

R

L

A

A

A

S

L

L

A

G

A

V

H

S

D

D

A

E

G

-

A

E

L

I

P

E

L

K

L

L

A

S

R

T

L

L

Y

Y

W

W

Y

F

T

T

V

V

E

E

F

F

G

G

L

L

I

C

R

K

D

Q

A

-

S

-

P

-

N

N

G

G

-

E

V

V

K

K

I

A

Y

Y

G

G

A

A

G

G

I

L

V

L

S

S

K

Y

G

G

E

E

T

L

L

L

Y

H

S

S

Q

-

Q

L

S

S

A

E

P

P

N

E

R

I

L

R

G

A

F

F

G

D

L

P

E

D

R

A

V

A

M

A

R

V

T

Q

R

P

Y

Y

R

Q

I

D

D

Q

T

T

F

Y

Q

Q

K

P

T

V

Y

Y

F

F

V

V

I

S

D

E

D

S

F

F

A

S

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
19 modified: Phosphoserine; by CaMK2
31 modified: Phosphoserine
40 modified: Phosphoserine; by CaMK2 and PKA

P04176 Phenylalanine-4-hydroxylase; PAH; Phe-4-monooxygenase; EC 1.14.16.1 from Rattus norvegicus (Rat) (see 2 papers)
33% identity, 74% coverage: 28:247/296 of query aligns to 175:393/453 of P04176

query
sites
P04176

P

P

T

R

E

V

R

E

Y

Y

G

T

A

E

V

E

D

E

H

K

A

Q

V

T

W

W

Q

G

Q

T

L

V

Y

F

A

R

R

T

Q

L

T

K

A

A

L

L

L

Y

K

K

G

T

R

H

V

A

C

C

D

Y

E

E

-

H

-

N

-

H

-

I

F

F

L

P

A

L

G

L

I

E

D

K

T

Y

I

C

G

G

M

F

P

R

P

E

D

D

R

N

V

I

P

P

S

Q

F

L

D

E

E

D

I

V

N

S

A

Q

K

F

L

L

A

Q

P

T

A

C

T

T

G

G

W

F

E

R

I

L

V

R

A

P

V

V

P

A

G

G

L

L

V

L

P

S

D

S

Q

R

V

D

F

F

F

L

E

G

H

G

L

L

A

A

N

F

R

R

R

V

F

F

P

H

V

C

T

T

W

Q

W

Y

M

I

R

R

R

H

P

G

D

S

Q

K

L

P

D

M

Y

Y

L

T

Q

P

E

E

P

P

D

D

C

I

F

C

H
|
H

D

E

L

L

F

L

G

G

H
|
H

V

V

P

P

L

L

L

F

I

S

N

D

P

R

V

S

F

F

A

A

D

Q

Y

F

M

S

H

Q

A

E

Y

I

G

G

R

L

A

A

A

S

L

L

A

G

A

A

H

P

D

D

A

E

G

-

A

Y

L

I

P

E

L

K

L

L

A

A

R

T

L

I

Y

Y

W

W

Y

F

T

T

V

V

E
|
E

F

F

G

G

L

L

I

C

R

K

D

E

A

G

A

D

S

S

P

-

N

-

G

-

V

I

K

K

I

A

Y

Y

G

G

A

A

G

G

I

L

V

L

S

S

K

F

G

G

E

E

T

L

L

Q

Y

Y

S

C

Q

-

Q

L

S

S

A

D

A

K

P

P

N

K

R

L

L

L

G

P

F

L

G

E

L

L

E

E

R

K

V

T

M

A

R

C

T

Q

R

E

Y

Y

R

S

I

V

D

T

T

E

F

F

Q

Q

K

P

T

L

Y

Y

F

Y

V

V

I

A

D

E

D

S

F

F

A

S

H285 (= H134) binding
H290 (= H139) binding
E330 (= E180) binding

Sites not aligning to the query:

16 modified: Phosphoserine; by PKA

5fgjA Structure of tetrameric rat phenylalanine hydroxylase, residues 1-453 (see paper)
33% identity, 74% coverage: 28:247/296 of query aligns to 153:371/428 of 5fgjA

query
sites
5fgjA

P

P

T

R

E

V

R

E

Y

Y

G

T

A

E

V

E

D

E

H

K

A

Q

V

T

W

W

Q

G

Q

T

L

V

Y

F

A

R

R

T

Q

L

T

K

A

A

L

L

L

Y

K

K

G

T

R

H

V

A

C

C

D

Y

E

E

-

H

-

N

-

H

-

I

F

F

L

P

A

L

G

L

I

E

D

K

T

Y

I

C

G

G

M

F

P

R

P

E

D

D

R

N

V

I

P

P

S

Q

F

L

D

E

E

D

I

V

N

S

A

Q

K

F

L

L

A

Q

P

T

A

C

T

T

G

G

W

F

E

R

I

L

V

R

A

P

V

V

P

A

G

G

L

L

V

L

P

S

D

S

Q

R

V

D

F

F

F

L

E

G

H

G

L

L

A

A

N

F

R

R

R

V

F

F

P

H

V

C

T

T

W

Q

W

Y

M

I

R

R

R

H

P

G

D

S

Q

K

L

P

D

M

Y

Y

L

T

Q

P

E

E

P

P

D

D

C

I

F

C

H
|
H

D

E

L

L

F

L

G

G

H
|
H

V

V

P

P

L

L

L

F

I

S

N

D

P

R

V

S

F

F

A

A

D

Q

Y

F

M

S

H

Q

A

E

Y

I

G

G

R

L

A

A

A

S

L

L

A

G

A

A

H

P

D

D

A

E

G

-

A

Y

L

I

P

E

L

K

L

L

A

A

R

T

L

I

Y

Y

W

W

Y

F

T

T

V

V

E
|
E

F

F

G

G

L

L

I

C

R

K

D

E

A

G

A

D

S

S

P

-

N

-

G

-

V

I

K

K

I

A

Y

Y

G

G

A

A

G

G

I

L

V

L

S
|
S

S

S

K

F

G

G

E

E

T

L

L

Q

Y

Y

S

C

Q

-

Q

L

S

S

A

D

A

K

P

P

N

K

R

L

L

L

G

P

F

L

G

E

L

L

E

E

R

K

V

T

M

A

R

C

T

Q

R

E

Y

Y

R

S

I

V

D

T

T

E

F

F

Q

Q

K

P

T

L

Y

Y

F

Y

V

V

I

A

D

E

D

S

F

F

A

S

active site: H263 (= H134), H268 (= H139), E308 (= E180), S327 (= S202)
binding fe (iii) ion: H263 (= H134), H268 (= H139), E308 (= E180)

P16331 Phenylalanine-4-hydroxylase; PAH; Phe-4-monooxygenase; EC 1.14.16.1 from Mus musculus (Mouse) (see paper)
34% identity, 74% coverage: 28:246/296 of query aligns to 175:392/453 of P16331

query
sites
P16331

P

P

T

R

E

V

R

E

Y

Y

G

T

A

E

V

E

D

E

H

R

A

K

V

T

W

W

Q

G

Q

T

L

V

Y

F

A

R

R

T

Q

L

T

K

A

A

L

L

L

Y

K

K

G

T

R

H

V

A

C

C

D

Y

E

E

-

H

-

N

-

H

-

I

F

F

L

P

A

L

G

L

I

E

D

K

T

Y

I

C

G

G

M

F

P

R

P

E

D

D

R

N

V

I

P

P

S

Q

F

L

D

E

E

D

I

V

N

S

A

Q

K

F

L

L

A

Q

P

T

A

C

T

T

G

G

W

F

E

R

I

L

V

R

A

P

V

V

P

A

G

G

L

L

V

L

P

S

D

S

Q

R

V

D

F

F

F

L

E

G

H

G

L

L

A

A

N

F

R

R

R

V

F
|
F

P

H

V

C

T

T

W

Q

W

Y

M

I

R

R

R

H

P

G

D

S

Q

K

L

P

D

M

Y

Y

L

T

Q

P

E

E

P

P

D

D

C

I

F

C

H

H

D

E

L

L

F

L

G

G

H

H

V

V

P

P

L

L

L

F

I

S

N

D

P

R

V

S

F

F

A

A

D

Q

Y

F

M

S

H

Q

A

E

Y

I

G

G

R

L

A

A

A

S

L

L

A

G

A

A

H

P

D

D

A

E

G

-

A

Y

L

I

P

E

L

K

L

L

A

A

R

T

L

I

Y

Y

W

W

Y

F

T

T

V

V

E

E

F

F

G

G

L

L

I

C

R

K

D

E

A

G

A

D

S

S

P

-

N

-

G

-

V

I

K

K

I

A

Y

Y

G

G

A

A

G

G

I

L

V

L

S

S

K

F

G

G

E

E

T

L

L

Q

Y

Y

S

C

Q

-

Q

L

S

S

A

D

A

K

P

P

N

K

R

L

L

L

G

P

F

L

G

E

L

L

E

E

R

K

V

T

M

A

R

C

T

Q

R

E

Y

Y

R

T

I

V

D

T

T

E

F

F

Q

Q

K

P

T

L

Y

Y

F

Y

V

V

I

A

D

E

D

S

F

F

F263 (= F112) mutation to S: Mutant mice have features of phenylketonuria.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
2 modified: N-acetylalanine
106 V→A: Mutant mice have mild features of phenylketonuria.

P00439 Phenylalanine-4-hydroxylase; PAH; Phe-4-monooxygenase; EC 1.14.16.1 from Homo sapiens (Human) (see 43 papers)
33% identity, 74% coverage: 28:246/296 of query aligns to 175:392/452 of P00439

query
sites
P00439

P

P

T
x
R

E
x
V

R
x
E

Y

Y

G

M

A

E

V

E

D

E

H

K

A

K

V

T

W

W

Q

G

Q

T

L
x
V

Y

F

A

K

R

T

Q

L

T

K

A

S

L

L

L

Y

K

K

G

T

R
x
H

V

A

C

C

D
x
Y

E

E

F

Y

L
x
N

A

H

G

I

I

F

D
x
P

T

L

I
x
L

-

E

-

K

-

Y

-

C

G
|
G

M

F

P

H

P
x
E

D
|
D

R

N

V
x
I

P
|
P

S

Q

F

L

D

E

E

D

I
x
V

N

S

A

Q

K
x
F

L

L

A

Q

P

T

A

C

T
|
T

G

G

W

F

E
x
R

I

L

V
x
R

A
x
P

V
|
V

P

A

G
|
G

L

L

V
x
L

P

S

D

S

Q
x
R

V

D

F

F

F
x
L

E

G

H

G

L

L

A
|
A

N

F

R
|
R

R

V

F

F

P

H

V

C

T

T

W

Q

W

Y

M
x
I

R
|
R

R

H

P

G

D
x
S

Q

K

L
x
P

D
x
M

Y
|
Y

L

T

Q

P

E
|
E

P
|
P

D
|
D

C
x
I

F

C

H

H

D

E

L

L

F

L

G

G

H

H

V

V

P

P

L

L

L

F

I

S

N

D

P
x
R

V

S

F
|
F

A
|
A

D

Q

Y

F

M
x
S

H

Q

A

E

Y
x
I

G

G

R

L

A
|
A

A
x
S

L
|
L

A

G

A

A

H
x
P

D

D

A

E

G

-

A

Y

L
x
I

P

E

L

K

L

L

A
|
A

R

T

L

I

Y

Y

W

W

Y

F

T

T

V

V

E

E

F
|
F

G

G

L

L

I

C

R

K

D

Q

A

G

A
x
D

S

S

P

-

N

-

G

-

V

I

K

K

I
x
A

Y

Y

G

G

A
|
A

G

G

I

L

V
x
L

S
|
S

K

F

G

G

E

E

T

L

L

Q

Y

Y

S

C

Q

-

Q

L

S

S

A

E

A

K

P

P

N

K

R
x
L

L

L

G

P

F

L

G

E

L

L

E

E

R

K

V

T

M

A

R

I

T

Q

R

N

Y
|
Y

R

T

I

V

D
x
T

T

E

F

F

Q

Q

K

P

T

L

Y

Y

F
x
Y

V
|
V

I

A

D
x
E

D

S

F

F

R176 (≠ T29) to L: in non-PKU HPA and PKU; dbSNP:rs74486803
V177 (≠ E30) to L: in PKU; haplotype 6; dbSNP:rs199475602
E178 (≠ R31) to G: in non-PKU HPA; dbSNP:rs77958223
V190 (≠ L43) to A: in PKU; haplotype 3; dbSNP:rs62514919
H201 (≠ R54) to Y: in non-PKU HPA; haplotype 1; dbSNP:rs62517205
Y204 (≠ D57) to C: in PKU; mild; haplotypes 3,4; dbSNP:rs62514927
N207 (≠ L60) to S: in PKU; severe; haplotype 4; dbSNP:rs62508721
P211 (≠ D64) to T: in PKU; haplotype 4; dbSNP:rs62514931
L213 (≠ I66) to P: in PKU; severe; dbSNP:rs62516109
G218 (= G67) to V: in PKU; haplotypes 1,2; dbSNP:rs62514933
E221 (≠ P70) to G: in PKU; haplotype 4; dbSNP:rs62514934
D222 (= D71) to V: in PKU; haplotypes 3,4; dbSNP:rs62507319
I224 (≠ V73) to M: in PKU; haplotype 4; dbSNP:rs199475576
P225 (= P74) to T: in PKU; haplotype 1; dbSNP:rs199475589
V230 (≠ I79) to I: in non-PKU HPA and PKU; haplotype 4; dbSNP:rs62516152
F233 (≠ K82) to L: in PKU; haplotypes 2,3; dbSNP:rs62517208
T238 (= T87) to P: in PKU; haplotype 4; dbSNP:rs199475577
R241 (≠ E90) to C: in non-PKU HPA and PKU; haplotype 34; dbSNP:rs76687508; to H: in PKU; haplotypes 1,5; dbSNP:rs62508730
R243 (≠ V92) to Q: in non-PKU HPA and PKU; haplotypes 4,7,9; dbSNP:rs62508588
P244 (≠ A93) to L: in PKU; haplotype 12; dbSNP:rs118203923
V245 (= V94) to A: in PKU, HPA and non-PKU HPA; haplotypes 3,7; dbSNP:rs796052017; to E: in PKU; haplotype 11; dbSNP:rs76212747
G247 (= G96) to V: in PKU; haplotype 4; dbSNP:rs199475579
L249 (≠ V98) to F: in PKU; haplotype 1; dbSNP:rs74503222
R252 (≠ Q101) to G: in PKU; haplotype 7; dbSNP:rs5030847; to Q: in PKU; haplotype 1; dbSNP:rs62644503; to W: in PKU; haplotypes 1,6,7,8,42, 69; complete loss of activity; dbSNP:rs5030847
L255 (≠ F104) to S: in PKU; haplotype 36; dbSNP:rs62642930; to V: in PKU; haplotypes 18,21; dbSNP:rs62642931
A259 (= A108) to T: in PKU; haplotype 3; dbSNP:rs62642932; to V: in PKU; haplotypes 7,42; dbSNP:rs118203921
R261 (= R110) to Q: in HPA and PKU; mild; haplotypes 1,2,4,22, 24,28; dbSNP:rs5030849
I269 (≠ M118) to L: in non-PKU HPA; dbSNP:rs62508692
R270 (= R119) to S: in PKU; haplotype 1; dbSNP:rs62514951
S273 (≠ D122) to F: in PKU; haplotype 7; dbSNP:rs62514953
P275 (≠ L124) to L: in PKU; reduced activity; increased affinity for the substrate; mildly reduced substrate activation; decreased cofactor affinity; dbSNP:rs62508715
M276 (≠ D125) to V: in PKU; haplotype 4; dbSNP:rs62516149
Y277 (= Y126) to D: in PKU; haplotype 2; dbSNP:rs78655458
E280 (= E129) to K: in PKU; haplotypes 1,2,4,16,38; partial residual activity; dbSNP:rs62508698
P281 (= P130) to L: in PKU; haplotypes 1,4; dbSNP:rs5030851
D282 (= D131) to N: in PKU; haplotype 1; dbSNP:rs199475582
I283 (≠ C132) to F: in PKU; haplotype 21; dbSNP:rs62517168; to N: in PKU; severe; dbSNP:rs62508693; mutation to C: Loss of positive cooperativity and reduction of fold-activation by L-Phe preincubation.
R297 (≠ P146) to C: in PKU; haplotype 4; dbSNP:rs62642945
F299 (= F148) to C: in PKU; haplotype 8; dbSNP:rs62642933
A300 (= A149) to S: in PKU and HPA; haplotype 1; does not affect oligomerization; reduction in activity is probably due to a global conformational change in the protein that reduces allostery; dbSNP:rs5030853
S303 (≠ M152) to P: in PKU; haplotype 5; dbSNP:rs199475608
I306 (≠ Y155) to V: in non-PKU HPA and PKU; haplotype 4; dbSNP:rs62642934
A309 (= A158) to D: in PKU; haplotype 7; dbSNP:rs62642935
S310 (≠ A159) to F: in PKU; haplotype 7; dbSNP:rs62642913; to Y: in HPA; reduction in activity is probably due to a global conformational change in the protein that reduces allostery; dbSNP:rs62642913
L311 (= L160) to P: in PKU; haplotypes 1,7,10; dbSNP:rs62642936
P314 (≠ H163) to S: in HPA; does not affect oligomerization; reduction in activity is probably due to a global conformational change in the protein that reduces allostery; dbSNP:rs199475650
I318 (≠ L168) to T: in PKU; partial loss of activity; dbSNP:rs62642918
A322 (= A172) to G: in PKU; haplotype 12; dbSNP:rs62514958; to T: in PKU; haplotype 1; dbSNP:rs62514957
F331 (= F181) to L: in PKU; haplotype 1; dbSNP:rs62517179
D338 (≠ A188) to Y: in PKU; haplotype 4; dbSNP:rs62516150
A342 (≠ I195) to T: in PKU; haplotype 5; dbSNP:rs62507282
A345 (= A198) to T: in PKU; haplotype 7; dbSNP:rs62516062
L348 (≠ V201) to V: in PKU; mild haplotype 9; dbSNP:rs62516092
S349 (= S202) to L: in PKU; severe; dbSNP:rs62507279; to P: in PKU; haplotypes 1,4; dbSNP:rs62508646
S350 (= S203) to T: in PKU; haplotype 2; dbSNP:rs62517183
L364 (≠ R218) natural variant: Missing (in PKU; haplotype 5; dbSNP:rs62516096)
Y377 (= Y231) to C: in PKU; haplotype 4; dbSNP:rs62642942
T380 (≠ D234) to M: in non-PKU HPA and PKU; haplotype 4; dbSNP:rs62642937
Y387 (≠ F241) to H: in PKU; haplotype 1; dbSNP:rs62517194
V388 (= V242) to M: in PKU; haplotypes 1,4; dbSNP:rs62516101
E390 (≠ D244) to G: in PKU and non-PKU HPA; haplotype 4; dbSNP:rs5030856

Sites not aligning to the query:

16 modified: Phosphoserine; by PKA; S → P: in PKU; uncertain significance; dbSNP:rs62642946
39 F → L: in HPA and PKU; haplotype 1; dbSNP:rs62642926; natural variant: Missing (in PKU; haplotypes 9,21)
41 L → P: in PKU; mild; dbSNP:rs62642916
42 K → I: in PKU; haplotype 21; dbSNP:rs62635346
46 G → S: in PKU; haplotype 5; significantly reduces phenylalanine binding; dbSNP:rs74603784
47 A → V: in non-PKU HPA; haplotype 4; significantly reduces phenylalanine binding; dbSNP:rs118203925
48 L → S: in PKU; mild; haplotypes 3,4; dbSNP:rs5030841
55 F → L: in HPA and PKU; does not affect oligomerization; results in loss of substrate activation; dbSNP:rs199475598
56 E → D: in PKU; haplotype 10; dbSNP:rs199475567
63:64 natural variant: TH -> PN (in PKU; haplotype 1; abolishes phenylalanine binding)
65 I → S: in PKU; results in disturbed oligomerization; results in loss of substrate activation; dbSNP:rs75193786; I → T: in PKU; haplotypes 1,5,9,21,B; abolishes phenylalanine binding; dbSNP:rs75193786; I → V: in HPA and PKU; dbSNP:rs199475643
67 S → P: in PKU; haplotype 4; dbSNP:rs5030842
68 R → S: in PKU; haplotype 1; dbSNP:rs76394784
76 E → G: in non-PKU HPA; dbSNP:rs62507347
84 D → Y: in PKU; haplotype 4; dbSNP:rs62514902
87 S → R: in non-PKU HPA; haplotype 1; dbSNP:rs62516151
94 natural variant: Missing (in PKU; mild; haplotype 2)
98 L → S: in non-PKU HPA; dbSNP:rs62517167
104 A → D: in PKU; mild; haplotype 1; dbSNP:rs62642929
124 T → I: in PKU; haplotype 28; dbSNP:rs199475571
143 D → G: in PKU; haplotype 11; dbSNP:rs199475572
148 G → S: in PKU; haplotypes 1,2,7; dbSNP:rs80297647
151 D → H: in PKU; haplotypes 1,8; dbSNP:rs199475597
157 R → N: in PKU; severe; 5% activity; requires 2 nucleotide substitutions; dbSNP:rs1565853495
158 R → Q: in PKU; haplotypes 1,2,4,7,16, 28; dbSNP:rs5030843
161 F → S: in PKU; haplotype 4; dbSNP:rs79635844
164 I → T: in PKU; haplotype 1; dbSNP:rs199475595
170 H → Q: in PKU; does not affect oligomerization; dbSNP:rs199475652
171 G → A: in PKU; haplotype 1; dbSNP:rs199475596
173 P → T: in PKU; haplotype 4; dbSNP:rs199475574
174 I → T: in PKU; haplotype 1; dbSNP:rs138809906
395 A → P: in PKU; haplotype 1; dbSNP:rs62516103
403 A → V: in non-PKU HPA and PKU; haplotype 43; dbSNP:rs5030857
408 R → Q: in PKU; haplotypes 4,12; dbSNP:rs5030859; R → W: in HPA and PKU; haplotypes 1,2,4,5,13,34,41,44; most common mutation; reduction in activity is probably due to a global conformational change in the protein that reduces allostery; dbSNP:rs5030858
410 F → S: in PKU; mild; dbSNP:rs62644475
413 R → P: in non-PKU HPA and PKU; haplotype 4; dbSNP:rs79931499; R → S: in PKU; haplotype 1; dbSNP:rs62644467
414 Y → C: in HPA and PKU; haplotype 4; does not affect oligomerization; reduction in activity is probably due to a global conformational change in the protein that reduces allostery; dbSNP:rs5030860
415 D → N: in PKU, HPA and non-PKU HPA; haplotype 1; dbSNP:rs62644499
417 Y → H: in PKU; reduction in activity is probably due to a global conformational change in the protein that reduces allostery; dbSNP:rs62644471
418 T → P: in PKU; haplotype 4; dbSNP:rs62644501

1kw0A Catalytic domain of human phenylalanine hydroxylase (fe(ii)) in complex with tetrahydrobiopterin and thienylalanine (see paper)
33% identity, 74% coverage: 28:246/296 of query aligns to 58:275/307 of 1kw0A

query
sites
1kw0A

P

P

T

R

E

V

R

E

Y

Y

G

M

A

E

V

E

D

E

H

K

A

K

V

T

W

W

Q

G

Q

T

L

V

Y

F

A

K

R

T

Q

L

T

K

A

S

L

L

L

Y

K

K

G

T

R

H

V

A

C

C

D

Y

E

E

F

Y

L

N

A

H

G

I

I

F

D

P

T

L

I

L

-

E

-

K

-

Y

-

C

G

G

M

F

P

H

P

E

D

D

R

N

V

I

P

P

S

Q

F

L

D

E

E

D

I

V

N

S

A

Q

K

F

L

L

A

Q

P

T

A

C

T

T

G

G

W

F

E

R

I

L

V

R

A

P

V

V

P

A

G

G

L
|
L

V
x
L

P

S

D
x
S

Q

R

V

D

F
|
F

F

L

E

G

H

G

L

L

A

A

N

F

R

R

R

V

F

F

P
x
H

V

C

T

T

W

Q

W

Y

M

I

R
|
R

R

H

P

G

D

S

Q

K

L

P

D

M

Y
|
Y

L
x
T

Q

P

E
|
E

P
|
P

D

D

C

I

F

C

H
|
H

D
x
E

L

L

F

L

G

G

H
|
H

V

V

P

P

L

L

L

F

I

S

N

D

P

R

V

S

F

F

A

A

D

Q

Y

F

M

S

H

Q

A

E

Y

I

G

G

R

L

A

A

A

S

L

L

A

G

A

A

H

P

D

D

A

E

G

-

A

Y

L

I

P

E

L

K

L

L

A

A

R

T

L

I

Y

Y

W

W

Y

F

T

T

V

V

E
|
E

F
|
F

G

G

L

L

I

C

R

K

D

Q

A

G

A

D

S

S

P

-

N

-

G

-

V

I

K

K

I

A

Y

Y

G

G

A

A

G

G

I

L

V

L

S
|
S

K

F

G

G

E

E

T

L

L

Q

Y

Y

S

C

Q

-

Q

L

S

S

A

E

A

K

P

P

N

K

R

L

L

L

G

P

F

L

G

E

L

L

E

E

R

K

V

T

M

A

R

I

T

Q

R

N

Y

Y

R

T

I

V

D

T

T

E

F

F

Q

Q

K

P

T

L

Y

Y

F

Y

V

V

I

A

D

E

D

S

F

F

active site: H168 (= H134), H173 (= H139), E213 (= E180), S232 (= S202)
binding fe (ii) ion: H168 (= H134), H173 (= H139), E213 (= E180)
binding 5,6,7,8-tetrahydrobiopterin: L131 (= L97), L132 (≠ V98), S134 (≠ D100), F137 (= F103), H147 (≠ P113), E169 (≠ D135), E213 (= E180)
binding beta(2-thienyl)alanine: R153 (= R119), Y160 (= Y126), T161 (≠ L127), E163 (= E129), P164 (= P130), H168 (= H134), F214 (= F181), S232 (= S202), S233 (= S203)

1j8uA Catalytic domain of human phenylalanine hydroxylase fe(ii) in complex with tetrahydrobiopterin (see paper)
33% identity, 74% coverage: 28:246/296 of query aligns to 58:275/307 of 1j8uA

query
sites
1j8uA

P

P

T

R

E

V

R

E

Y

Y

G

M

A

E

V

E

D

E

H

K

A

K

V

T

W

W

Q

G

Q

T

L

V

Y

F

A

K

R

T

Q

L

T

K

A

S

L

L

L

Y

K

K

G

T

R

H

V

A

C

C

D

Y

E

E

F

Y

L

N

A

H

G

I

I

F

D

P

T

L

I

L

-

E

-

K

-

Y

-

C

G

G

M

F

P

H

P

E

D

D

R

N

V

I

P

P

S

Q

F

L

D

E

E

D

I

V

N

S

A

Q

K

F

L

L

A

Q

P

T

A

C

T

T

G

G

W

F

E

R

I

L

V

R

A

P

V

V

P

A

G

G

L

L

V
x
L

P

S

D
x
S

Q

R

V

D

F
|
F

F
x
L

E

G

H

G

L

L

A

A

N

F

R

R

R

V

F

F

P

H

V

C

T

T

W

Q

W

Y

M

I

R

R

R

H

P

G

D

S

Q

K

L

P

D

M

Y

Y

L

T

Q

P

E

E

P

P

D

D

C

I

F

C

H
|
H

D

E

L

L

F

L

G

G

H
|
H

V

V

P

P

L

L

L

F

I

S

N

D

P

R

V

S

F

F

A

A

D

Q

Y

F

M

S

H

Q

A

E

Y

I

G

G

R

L

A

A

A

S

L

L

A

G

A

A

H

P

D

D

A

E

G

-

A

Y

L

I

P

E

L

K

L

L

A
|
A

R

T

L

I

Y

Y

W

W

Y

F

T

T

V

V

E
|
E

F

F

G

G

L

L

I

C

R

K

D

Q

A

G

A

D

S

S

P

-

N

-

G

-

V

I

K

K

I

A

Y

Y

G

G

A

A

G

G

I

L

V

L

S
|
S

S

S

K

F

G

G

E

E

T

L

L

Q

Y

Y

S

C

Q

-

Q

L

S

S

A

E

A

K

P

P

N

K

R

L

L

L

G

P

F

L

G

E

L

L

E

E

R

K

V

T

M

A

R

I

T

Q

R

N

Y

Y

R

T

I

V

D

T

T

E

F

F

Q

Q

K

P

T

L

Y

Y

F

Y

V

V

I

A

D

E

D

S

F

F

active site: H168 (= H134), H173 (= H139), E213 (= E180), S232 (= S202)
binding fe (ii) ion: H168 (= H134), H173 (= H139), E213 (= E180)
binding 5,6,7,8-tetrahydrobiopterin: L132 (≠ V98), S134 (≠ D100), F137 (= F103), L138 (≠ F104), A205 (= A172)

Query Sequence

>BPHYT_RS19520 FitnessBrowser__BFirm:BPHYT_RS19520
MSTANTAKLKEQFHAGLETRADFTIDQPTERYGAVDHAVWQQLYARQTALLKGRVCDEFL
AGIDTIGMPPDRVPSFDEINAKLAPATGWEIVAVPGLVPDQVFFEHLANRRFPVTWWMRR
PDQLDYLQEPDCFHDLFGHVPLLINPVFADYMHAYGRAALAAHDAGALPLLARLYWYTVE
FGLIRDAASPNGVKIYGAGIVSSKGETLYSQQSAAPNRLGFGLERVMRTRYRIDTFQKTY
FVIDDFAQLFKVAQTDFAPLLAKLVAEPALAAGDVLEHDRVITRGSQEGWLADGDI

Or try a new SitesBLAST search

SitesBLAST's Database

SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory