SitesBLAST

3tcyA Crystallographic structure of phenylalanine hydroxylase from chromobacterium violaceum (cpah) bound to phenylalanine in a site distal to the active site (see paper)
60% identity, 88% coverage: 17:274/294 of query aligns to 20:277/277 of 3tcyA

query
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3tcyA

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active site: H132 (= H129), H137 (= H134), E178 (= E175), S197 (= S194)
binding cobalt (ii) ion: H132 (= H129), H137 (= H134), E178 (= E175)
binding phenylalanine: A152 (= A149), Y153 (= Y150), K159 (≠ R156), L169 (= L166), T248 (= T245), P250 (≠ R247), D251 (= D248), F252 (= F249)

4etlA Crystallographic structure of phenylalanine hydroxylase from chromobacterium violaceum f258a mutation (see paper)
59% identity, 88% coverage: 17:274/294 of query aligns to 20:277/277 of 4etlA

query
sites
4etlA

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active site: H132 (= H129), H137 (= H134), E178 (= E175), S197 (= S194)
binding cobalt (ii) ion: H132 (= H129), H137 (= H134), E178 (= E175)

1ltzA Crystal structure of chromobacterium violaceum phenylalanine hydroxylase, structure has bound iron (iii) and oxidized cofactor 7, 8-dihydrobiopterin (see paper)
59% identity, 88% coverage: 17:274/294 of query aligns to 20:274/274 of 1ltzA

query
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1ltzA

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active site: H132 (= H129), H137 (= H134), E178 (= E175), S197 (= S194)
binding fe (iii) ion: H132 (= H129), H137 (= H134), E178 (= E175)
binding 7,8-dihydrobiopterin: I96 (≠ V93), D98 (= D95), F101 (= F98), Y173 (= Y170)

2v27B Structure of the cold active phenylalanine hydroxylase from colwellia psychrerythraea 34h (see paper)
41% identity, 84% coverage: 21:266/294 of query aligns to 11:255/272 of 2v27B

query
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2v27B

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active site: H119 (= H129), H124 (= H134), E164 (= E175), S183 (= S194)
binding fe (iii) ion: H119 (= H129), H124 (= H134), E164 (= E175)

5jk5A Phenylalanine hydroxylase from dictyostelium - bh2 complex
34% identity, 79% coverage: 27:259/294 of query aligns to 153:386/400 of 5jk5A

query
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A

Q

K

E

E

V

-

T

Q

L

M

R
|
R

D

Q

F

F

G

A

A

D

I

S

Y

F

E

K

R

K

L

P

A

F

S

S

V

I

active site: H259 (= H129), H264 (= H134), E304 (= E175), S323 (= S194)
binding fe (iii) ion: H259 (= H129), H264 (= H134), E304 (= E175)
binding 7,8-dihydrobiopterin: G221 (= G91), L222 (= L92), L223 (≠ V93), F228 (= F98), L229 (≠ F99), S296 (≠ A167), Y299 (= Y170)
binding piperazine-n,n'-bis(2-ethanesulfonic acid): T212 (= T82), P271 (= P141), D275 (= D145), R374 (= R247)

5jk8A Phenylalanine hydroxylase from dictyostelium - bh2, norleucine complex
34% identity, 79% coverage: 27:259/294 of query aligns to 144:377/390 of 5jk8A

query
sites
5jk8A

Y

Y

T

T

Q

E

A

E

E

E

H

I

D

K

V

T

W

W

I

G

T

V

L

V

Y

Y

E

N

R

R

Q

L

T

K

D

E

M

L

L

F

H

P

G

T

R

N

A

A

C

C

D

H

E

Q

F

H

M

A

R

Y

G

I

L

F

D

P

A

L

L

L

D

E

L

Q

H

N

R

C

-

G

-

Y

-

S

-

P

S

D

G

N

I

I

P

P

D

Q

F

L

A

Q

R

D

I

I

N

S

E

N

E

F

L

L

K

Q

R

E

L

C

T
|
T

G

G

W

W

T

R

V

I

V

R

A

P

V

V

P

Q

G

G

L

L

V
x
L

P

S

D
x
A

D

R

V

D

F
|
F

F

L

D

N

H

G

L

L

A

A

N

F

R
|
R

R

V

F

F

P

H

A

A

G

T

Q

Q

F

Y

I

I

R

R

K

H

P

P

H

S

E

V

L

P

D

L

Y
|
Y

L
x
T

Q

P

E

E

P

P

D

D

I

C

F

C

H
|
H

D

E

V

L

F

L

G

G

H
|
H

V

V

P

P

M

L

L

L

T

A

D

D

P

P

V

D

F

F

A

A

D
|
D

Y

F

M

S

Q

Q

A

-

Y

-

G

-

E

E

G

I

G

G

R

L

R

A

A

S

L

I

G

G

L

A

G

S

-

D

-

E

R

D

L

I

A

Q

N

L

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

M

C

N

K

T

E

P

G

A

D

G

T

L

I

R

R

I

A

Y

Y

G

G

A

A

G

G

I

I

V

L

S
|
S

R

T

T

G

E

E

S

M

I

E

F

H

A

F

L

L

D

T

D

D

P

K

S

A

P

-

N

K

R

K

I

L

G

P

F

F

D

N

L

P

E

F

R

D

V

A

M

C

R

N

T

T

L

E

Y

Y

R

P

I

I

D

T

F

F

Q

Q

Q

P

V

L

Y

Y

F

Y

V

V

I

A

D

E

S

S

I

F

Q

Q

T

K

L

A

Q

K

E

E

V

-

T

Q

L

M

R
|
R

D

Q

F

F

G

A

A

D

I

S

Y

F

E

K

R

K

L

P

A

F

S

S

V

I

active site: H250 (= H129), H255 (= H134), E295 (= E175), S314 (= S194)
binding fe (iii) ion: H250 (= H129), H255 (= H134), E295 (= E175)
binding 7,8-dihydrobiopterin: L214 (≠ V93), A216 (≠ D95), F219 (= F98), S287 (≠ A167), Y290 (= Y170)
binding norleucine: Y242 (= Y121), T243 (≠ L122), H250 (= H129), S314 (= S194), S315 (= S195)
binding piperazine-n,n'-bis(2-ethanesulfonic acid): T203 (= T82), R226 (= R105), D266 (= D145), R365 (= R247)

Sites not aligning to the query:

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

1tg2A Crystal structure of phenylalanine hydroxylase a313t mutant with 7,8- dihydrobiopterin bound (see paper)
32% identity, 79% coverage: 27:259/294 of query aligns to 63:296/308 of 1tg2A

query
sites
1tg2A

Y

Y

T

M

Q

E

A

E

E

E

H

K

D

K

V

T

W

W

I

G

T

T

L

V

Y

F

E

K

R

T

Q

L

T

K

D

S

M

L

L

Y

H

K

G

T

R

H

A

A

C

C

D

Y

E

E

F

Y

M

N

R

H

G

I

L

F

D

P

A

L

L

L

D

E

-

K

-

Y

-

C

-

G

L

F

H

H

R

E

S

D

G

N

I

I

P

P

D

Q

F

L

A

E

R

D

I

V

N

S

E

Q

E

F

L

L

K

Q

R

T

L

C

T

T

G

G

W

F

T

R

V

L

V

R

A

P

V

V

P

A

G

G

L

L

V
x
L

P

S

D
x
S

D

R

V

D

F
|
F

F

L

D

G

H

G

L

L

A

A

N

F

R

R

R

V

F

F

P

H

A

C

G

T

Q

Q

F

Y

I

I

R

R

K

H

P

G

H

S

E

K

L

P

D

M

Y

Y

L

T

Q

P

E

E

P

P

D

D

I

I

F

C

H
|
H

D

E

V

L

F

L

G

G

H
|
H

V

V

P

P

M

L

L

F

T

S

D

D

P

R

V

S

F

F

A

A

D

Q

Y

F

M

S

Q

Q

A

-

Y

-

G

-

E

E

G

I

G

G

R

L

R

A

A

S

L

L

G

G

L

T

-

P

-

D

G

E

R

Y

L

I

A

E

N

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

M

C

N

K

T

Q

P

G

A

D

G

S

L

I

R

K

I

A

Y

Y

G

G

A

A

G

G

I

L

V

L

S
|
S

S

S

R

F

T

G

E

E

S

L

I

Q

F

Y

A

C

L

L

D

S

D

E

P

-

S

K

P

P

N

K

R

L

I

L

G

P

F

L

D

E

L

L

E

E

R

K

V

T

M

A

R

I

T

Q

L

N

Y

Y

R

T

I

V

D

T

D

E

F

F

Q

Q

Q

P

V

L

Y

Y

F

Y

V

V

I

A

D

E

S

S

I

F

Q

N

T

D

L

A

Q

K

E

E

V

-

T

K

L

V

R

R

D

N

F

F

G

A

A

A

I

T

Y

I

E

P

R

R

L

P

A

F

S

S

V

V

active site: H169 (= H129), H174 (= H134), E214 (= E175), S233 (= S194)
binding fe (iii) ion: H169 (= H129), H174 (= H134), E214 (= E175)
binding 2-amino-6-(1,2-dihydroxy-propyl)-7,8-dihydro-6h-pteridin-4-one: L133 (≠ V93), S135 (≠ D95), F138 (= F98), Y209 (= Y170)

6pahA Human phenylalanine hydroxylase catalytic domain dimer with bound l- dopa (3,4-dihydroxyphenylalanine) inhibitor (see paper)
32% identity, 79% coverage: 27:259/294 of query aligns to 63:296/308 of 6pahA

query
sites
6pahA

Y

Y

T

M

Q

E

A

E

E

E

H

K

D

K

V

T

W

W

I

G

T

T

L

V

Y

F

E

K

R

T

Q

L

T

K

D

S

M

L

L

Y

H

K

G

T

R

H

A

A

C

C

D

Y

E

E

F

Y

M

N

R

H

G

I

L

F

D

P

A

L

L

L

D

E

-

K

-

Y

-

C

-

G

L

F

H

H

R

E

S

D

G

N

I

I

P

P

D

Q

F

L

A

E

R

D

I

V

N

S

E

Q

E

F

L

L

K

Q

R

T

L

C

T

T

G

G

W

F

T

R

V

L

V

R

A

P

V

V

P

A

G

G

L

L

V

L

P

S

D

S

D

R

V

D

F

F

F

L

D

G

H

G

L

L

A

A

N

F

R

R

R

V

F

F

P

H

A

C

G

T

Q

Q

F

Y

I

I

R

R

K

H

P

G

H

S

E

K

L

P

D

M

Y

Y

L

T

Q

P

E

E

P

P

D

D

I

I

F

C

H
|
H

D

E

V

L

F

L

G

G

H
|
H

V

V

P

P

M

L

L

F

T

S

D

D

P

R

V

S

F

F

A

A

D

Q

Y

F

M

S

Q

Q

A

-

Y

-

G

-

E

E

G

I

G

G

R

L

R

A

A

S

L

L

G

G

L

A

-

P

-

D

G

E

R

Y

L

I

A

E

N

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

M

C

N

K

T

Q

P

G

A

D

G

S

L

I

R

K

I

A

Y

Y

G

G

A

A

G

G

I

L

V

L

S
|
S

S

S

R

F

T

G

E

E

S

L

I

Q

F

Y

A

C

L

L

D

S

D

E

P

-

S

K

P

P

N

K

R

L

I

L

G

P

F

L

D

E

L

L

E

E

R

K

V

T

M

A

R

I

T

Q

L

N

Y

Y

R

T

I

V

D

T

D

E

F

F

Q

Q

Q

P

V

L

Y

Y

F

Y

V

V

I

A

D

E

S

S

I

F

Q

N

T

D

L

A

Q

K

E

E

V

-

T

K

L

V

R

R

D

N

F

F

G

A

A

A

I

T

Y

I

E

P

R

R

L

P

A

F

S

S

V

V

active site: H169 (= H129), H174 (= H134), E214 (= E175), S233 (= S194)
binding 3,4-dihydroxyphenylalanine: H169 (= H129), H174 (= H134), Y209 (= Y170), E214 (= E175)
binding fe (iii) ion: H169 (= H129), H174 (= H134), E214 (= E175)

5pahA Human phenylalanine hydroxylase catalytic domain dimer with bound dopamine inhibitor (see paper)
32% identity, 79% coverage: 27:259/294 of query aligns to 63:296/308 of 5pahA

query
sites
5pahA

Y

Y

T

M

Q

E

A

E

E

E

H

K

D

K

V

T

W

W

I

G

T

T

L

V

Y

F

E

K

R

T

Q

L

T

K

D

S

M

L

L

Y

H

K

G

T

R

H

A

A

C

C

D

Y

E

E

F

Y

M

N

R

H

G

I

L

F

D

P

A

L

L

L

D

E

-

K

-

Y

-

C

-

G

L

F

H

H

R

E

S

D

G

N

I

I

P

P

D

Q

F

L

A

E

R

D

I

V

N

S

E

Q

E

F

L

L

K

Q

R

T

L

C

T

T

G

G

W

F

T

R

V

L

V

R

A

P

V

V

P

A

G

G

L

L

V

L

P

S

D

S

D

R

V

D

F

F

F

L

D

G

H

G

L

L

A

A

N

F

R

R

R

V

F

F

P

H

A

C

G

T

Q

Q

F

Y

I

I

R

R

K

H

P

G

H

S

E

K

L

P

D

M

Y

Y

L

T

Q

P

E

E

P

P

D

D

I

I

F

C

H
|
H

D

E

V

L

F

L

G

G

H
|
H

V

V

P

P

M

L

L

F

T

S

D

D

P

R

V

S

F

F

A

A

D

Q

Y

F

M

S

Q

Q

A

-

Y

-

G

-

E

E

G

I

G

G

R

L

R

A

A

S

L

L

G

G

L

A

-

P

-

D

G

E

R

Y

L

I

A

E

N

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

M

C

N

K

T

Q

P

G

A

D

G

S

L

I

R

K

I

A

Y

Y

G

G

A

A

G

G

I

L

V

L

S
|
S

S

S

R

F

T

G

E

E

S

L

I

Q

F

Y

A

C

L

L

D

S

D

E

P

-

S

K

P

P

N

K

R

L

I

L

G

P

F

L

D

E

L

L

E

E

R

K

V

T

M

A

R

I

T

Q

L

N

Y

Y

R

T

I

V

D

T

D

E

F

F

Q

Q

Q

P

V

L

Y

Y

F

Y

V

V

I

A

D

E

S

S

I

F

Q

N

T

D

L

A

Q

K

E

E

V

-

T

K

L

V

R

R

D

N

F

F

G

A

A

A

I

T

Y

I

E

P

R

R

L

P

A

F

S

S

V

V

active site: H169 (= H129), H174 (= H134), E214 (= E175), S233 (= S194)
binding fe (iii) ion: H169 (= H129), H174 (= H134), E214 (= E175)
binding l-dopamine: H169 (= H129), H174 (= H134), Y209 (= Y170), E214 (= E175)

4pahA Human phenylalanine hydroxylase catalytic domain dimer with bound nor- adrenaline inhibitor (see paper)
32% identity, 79% coverage: 27:259/294 of query aligns to 63:296/308 of 4pahA

query
sites
4pahA

Y

Y

T

M

Q

E

A

E

E

E

H

K

D

K

V

T

W

W

I

G

T

T

L

V

Y

F

E

K

R

T

Q

L

T

K

D

S

M

L

L

Y

H

K

G

T

R

H

A

A

C

C

D

Y

E

E

F

Y

M

N

R

H

G

I

L

F

D

P

A

L

L

L

D

E

-

K

-

Y

-

C

-

G

L

F

H

H

R

E

S

D

G

N

I

I

P

P

D

Q

F

L

A

E

R

D

I

V

N

S

E

Q

E

F

L

L

K

Q

R

T

L

C

T

T

G

G

W

F

T

R

V

L

V

R

A

P

V

V

P

A

G

G

L

L

V

L

P

S

D

S

D

R

V

D

F
|
F

F

L

D

G

H

G

L

L

A

A

N

F

R

R

R

V

F

F

P

H

A

C

G

T

Q

Q

F

Y

I

I

R

R

K

H

P

G

H

S

E

K

L

P

D

M

Y

Y

L

T

Q

P

E

E

P

P

D

D

I

I

F

C

H
|
H

D

E

V

L

F

L

G

G

H
|
H

V

V

P

P

M

L

L

F

T

S

D

D

P

R

V

S

F

F

A

A

D

Q

Y

F

M

S

Q

Q

A

-

Y

-

G

-

E

E

G

I

G

G

R

L

R

A

A

S

L

L

G

G

L

A

-

P

-

D

G

E

R

Y

L

I

A

E

N

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

M

C

N

K

T

Q

P

G

A

D

G

S

L

I

R

K

I

A

Y

Y

G

G

A

A

G

G

I

L

V

L

S
|
S

S

S

R

F

T

G

E

E

S

L

I

Q

F

Y

A

C

L

L

D

S

D

E

P

-

S

K

P

P

N

K

R

L

I

L

G

P

F

L

D

E

L

L

E

E

R

K

V

T

M

A

R

I

T

Q

L

N

Y

Y

R

T

I

V

D

T

D

E

F

F

Q

Q

Q

P

V

L

Y

Y

F

Y

V

V

I

A

D

E

S

S

I

F

Q

N

T

D

L

A

Q

K

E

E

V

-

T

K

L

V

R

R

D

N

F

F

G

A

A

A

I

T

Y

I

E

P

R

R

L

P

A

F

S

S

V

V

active site: H169 (= H129), H174 (= H134), E214 (= E175), S233 (= S194)
binding fe (iii) ion: H169 (= H129), H174 (= H134), E214 (= E175)
binding l-norepinephrine: F138 (= F98), H169 (= H129), H174 (= H134), Y209 (= Y170), E214 (= E175)

3pahA Human phenylalanine hydroxylase catalytic domain dimer with bound adrenaline inhibitor (see paper)
32% identity, 79% coverage: 27:259/294 of query aligns to 63:296/308 of 3pahA

query
sites
3pahA

Y

Y

T

M

Q

E

A

E

E

E

H

K

D

K

V

T

W

W

I

G

T

T

L

V

Y

F

E

K

R

T

Q

L

T

K

D

S

M

L

L

Y

H

K

G

T

R

H

A

A

C

C

D

Y

E

E

F

Y

M

N

R

H

G

I

L

F

D

P

A

L

L

L

D

E

-

K

-

Y

-

C

-

G

L

F

H

H

R

E

S

D

G

N

I

I

P

P

D

Q

F

L

A

E

R

D

I

V

N

S

E

Q

E

F

L

L

K

Q

R

T

L

C

T

T

G

G

W

F

T

R

V

L

V

R

A

P

V

V

P

A

G

G

L
|
L

V

L

P

S

D

S

D

R

V

D

F

F

F

L

D

G

H

G

L

L

A

A

N

F

R

R

R

V

F

F

P

H

A

C

G

T

Q

Q

F

Y

I

I

R

R

K

H

P

G

H

S

E

K

L

P

D

M

Y

Y

L

T

Q

P

E

E

P

P

D

D

I

I

F

C

H
|
H

D

E

V

L

F

L

G

G

H
|
H

V

V

P

P

M

L

L

F

T

S

D

D

P

R

V

S

F

F

A

A

D

Q

Y

F

M

S

Q

Q

A

-

Y

-

G

-

E

E

G

I

G

G

R

L

R

A

A

S

L

L

G

G

L

A

-

P

-

D

G

E

R

Y

L

I

A

E

N

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

M

C

N

K

T

Q

P

G

A

D

G

S

L

I

R

K

I

A

Y

Y

G

G

A

A

G

G

I

L

V

L

S
|
S

S

S

R

F

T

G

E

E

S

L

I

Q

F

Y

A

C

L

L

D

S

D

E

P

-

S

K

P

P

N

K

R

L

I

L

G

P

F

L

D

E

L

L

E

E

R

K

V

T

M

A

R

I

T

Q

L

N

Y

Y

R

T

I

V

D

T

D

E

F

F

Q

Q

Q

P

V

L

Y

Y

F

Y

V

V

I

A

D

E

S

S

I

F

Q

N

T

D

L

A

Q

K

E

E

V

-

T

K

L

V

R

R

D

N

F

F

G

A

A

A

I

T

Y

I

E

P

R

R

L

P

A

F

S

S

V

V

active site: H169 (= H129), H174 (= H134), E214 (= E175), S233 (= S194)
binding fe (iii) ion: H169 (= H129), H174 (= H134), E214 (= E175)
binding 4-[(1S)-1-hydroxy-2-(methylamino)ethyl]benzene-1,2-diol: L132 (= L92), H174 (= H134), Y209 (= Y170), E214 (= E175)

1mmtA Crystal structure of ternary complex of the catalytic domain of human phenylalanine hydroxylase (fe(ii)) complexed with tetrahydrobiopterin and norleucine (see paper)
32% identity, 79% coverage: 27:259/294 of query aligns to 63:296/308 of 1mmtA

query
sites
1mmtA

Y

Y

T

M

Q

E

A

E

E

E

H

K

D

K

V

T

W

W

I

G

T

T

L

V

Y

F

E

K

R

T

Q

L

T

K

D

S

M

L

L

Y

H

K

G

T

R

H

A

A

C

C

D

Y

E

E

F

Y

M

N

R

H

G

I

L

F

D

P

A

L

L

L

D

E

-

K

-

Y

-

C

-

G

L

F

H

H

R

E

S

D

G

N

I

I

P

P

D

Q

F

L

A

E

R

D

I

V

N

S

E

Q

E

F

L

L

K

Q

R

T

L

C

T

T

G

G

W

F

T

R

V

L

V

R

A

P

V

V

P

A

G
|
G

L
|
L

V
x
L

P

S

D
x
S

D

R

V

D

F
|
F

F
x
L

D

G

H

G

L

L

A

A

N

F

R

R

R

V

F

F

P
x
H

A

C

G

T

Q

Q

F

Y

I

I

R
|
R

K

H

P

G

H

S

E

K

L

P

D

M

Y
|
Y

L
x
T

Q

P

E

E

P

P

D

D

I

I

F

C

H
|
H

D
x
E

V

L

F

L

G

G

H
|
H

V

V

P

P

M

L

L

F

T

S

D

D

P

R

V

S

F

F

A

A

D

Q

Y

F

M

S

Q

Q

A

-

Y

-

G

-

E

E

G

I

G

G

R

L

R

A

A

S

L

L

G

G

L

A

-

P

-

D

G

E

R

Y

L

I

A

E

N

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

M

C

N

K

T

Q

P

G

A

D

G

S

L

I

R

K

I

A

Y

Y

G

G

A

A

G

G

I

L

V

L

S
|
S

R

F

T

G

E

E

S

L

I

Q

F

Y

A

C

L

L

D

S

D

E

P

-

S

K

P

P

N

K

R

L

I

L

G

P

F

L

D

E

L

L

E

E

R

K

V

T

M

A

R

I

T

Q

L

N

Y

Y

R

T

I

V

D

T

D

E

F

F

Q

Q

Q

P

V

L

Y

Y

F

Y

V

V

I

A

D

E

S

S

I

F

Q

N

T

D

L

A

Q

K

E

E

V

-

T

K

L

V

R

R

D

N

F

F

G

A

A

A

I

T

Y

I

E

P

R

R

L

P

A

F

S

S

V

V

active site: H169 (= H129), H174 (= H134), E214 (= E175), S233 (= S194)
binding fe (ii) ion: H169 (= H129), H174 (= H134), E214 (= E175)
binding 5,6,7,8-tetrahydrobiopterin: G131 (= G91), L132 (= L92), L133 (≠ V93), S135 (≠ D95), F138 (= F98), L139 (≠ F99), H148 (≠ P108), E170 (≠ D130), Y209 (= Y170), E214 (= E175)
binding norleucine: R154 (= R114), Y161 (= Y121), T162 (≠ L122), H169 (= H129), S233 (= S194), S234 (= S195)

1kw0A Catalytic domain of human phenylalanine hydroxylase (fe(ii)) in complex with tetrahydrobiopterin and thienylalanine (see paper)
32% identity, 79% coverage: 27:259/294 of query aligns to 62:295/307 of 1kw0A

query
sites
1kw0A

Y

Y

T

M

Q

E

A

E

E

E

H

K

D

K

V

T

W

W

I

G

T

T

L

V

Y

F

E

K

R

T

Q

L

T

K

D

S

M

L

L

Y

H

K

G

T

R

H

A

A

C

C

D

Y

E

E

F

Y

M

N

R

H

G

I

L

F

D

P

A

L

L

L

D

E

-

K

-

Y

-

C

-

G

L

F

H

H

R

E

S

D

G

N

I

I

P

P

D

Q

F

L

A

E

R

D

I

V

N

S

E

Q

E

F

L

L

K

Q

R

T

L

C

T

T

G

G

W

F

T

R

V

L

V

R

A

P

V

V

P

A

G

G

L
|
L

V
x
L

P

S

D
x
S

D

R

V

D

F
|
F

F

L

D

G

H

G

L

L

A

A

N

F

R

R

R

V

F

F

P
x
H

A

C

G

T

Q

Q

F

Y

I

I

R
|
R

K

H

P

G

H

S

E

K

L

P

D

M

Y
|
Y

L
x
T

Q

P

E
|
E

P
|
P

D

D

I

I

F

C

H
|
H

D
x
E

V

L

F

L

G

G

H
|
H

V

V

P

P

M

L

L

F

T

S

D

D

P

R

V

S

F

F

A

A

D

Q

Y

F

M

S

Q

Q

A

-

Y

-

G

-

E

E

G

I

G

G

R

L

R

A

A

S

L

L

G

G

L

A

-

P

-

D

G

E

R

Y

L

I

A

E

N

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

M

C

N

K

T

Q

P

G

A

D

G

S

L

I

R

K

I

A

Y

Y

G

G

A

A

G

G

I

L

V

L

S
|
S

R

F

T

G

E

E

S

L

I

Q

F

Y

A

C

L

L

D

S

D

E

P

-

S

K

P

P

N

K

R

L

I

L

G

P

F

L

D

E

L

L

E

E

R

K

V

T

M

A

R

I

T

Q

L

N

Y

Y

R

T

I

V

D

T

D

E

F

F

Q

Q

Q

P

V

L

Y

Y

F

Y

V

V

I

A

D

E

S

S

I

F

Q

N

T

D

L

A

Q

K

E

E

V

-

T

K

L

V

R

R

D

N

F

F

G

A

A

A

I

T

Y

I

E

P

R

R

L

P

A

F

S

S

V

V

active site: H168 (= H129), H173 (= H134), E213 (= E175), S232 (= S194)
binding fe (ii) ion: H168 (= H129), H173 (= H134), E213 (= E175)
binding 5,6,7,8-tetrahydrobiopterin: L131 (= L92), L132 (≠ V93), S134 (≠ D95), F137 (= F98), H147 (≠ P108), E169 (≠ D130), E213 (= E175)
binding beta(2-thienyl)alanine: R153 (= R114), Y160 (= Y121), T161 (≠ L122), E163 (= E124), P164 (= P125), H168 (= H129), F214 (= F176), S232 (= S194), S233 (= S195)

1j8uA Catalytic domain of human phenylalanine hydroxylase fe(ii) in complex with tetrahydrobiopterin (see paper)
32% identity, 79% coverage: 27:259/294 of query aligns to 62:295/307 of 1j8uA

query
sites
1j8uA

Y

Y

T

M

Q

E

A

E

E

E

H

K

D

K

V

T

W

W

I

G

T

T

L

V

Y

F

E

K

R

T

Q

L

T

K

D

S

M

L

L

Y

H

K

G

T

R

H

A

A

C

C

D

Y

E

E

F

Y

M

N

R

H

G

I

L

F

D

P

A

L

L

L

D

E

-

K

-

Y

-

C

-

G

L

F

H

H

R

E

S

D

G

N

I

I

P

P

D

Q

F

L

A

E

R

D

I

V

N

S

E

Q

E

F

L

L

K

Q

R

T

L

C

T

T

G

G

W

F

T

R

V

L

V

R

A

P

V

V

P

A

G

G

L

L

V
x
L

P

S

D
x
S

D

R

V

D

F
|
F

F
x
L

D

G

H

G

L

L

A

A

N

F

R

R

R

V

F

F

P

H

A

C

G

T

Q

Q

F

Y

I

I

R

R

K

H

P

G

H

S

E

K

L

P

D

M

Y

Y

L

T

Q

P

E

E

P

P

D

D

I

I

F

C

H
|
H

D

E

V

L

F

L

G

G

H
|
H

V

V

P

P

M

L

L

F

T

S

D

D

P

R

V

S

F

F

A

A

D

Q

Y

F

M

S

Q

Q

A

-

Y

-

G

-

E

E

G

I

G

G

R

L

R

A

A

S

L

L

G

G

L

A

-

P

-

D

G

E

R

Y

L

I

A

E

N

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

M

C

N

K

T

Q

P

G

A

D

G

S

L

I

R

K

I

A

Y

Y

G

G

A

A

G

G

I

L

V

L

S
|
S

S

S

R

F

T

G

E

E

S

L

I

Q

F

Y

A

C

L

L

D

S

D

E

P

-

S

K

P

P

N

K

R

L

I

L

G

P

F

L

D

E

L

L

E

E

R

K

V

T

M

A

R

I

T

Q

L

N

Y

Y

R

T

I

V

D

T

D

E

F

F

Q

Q

Q

P

V

L

Y

Y

F

Y

V

V

I

A

D

E

S

S

I

F

Q

N

T

D

L

A

Q

K

E

E

V

-

T

K

L

V

R

R

D

N

F

F

G

A

A

A

I

T

Y

I

E

P

R

R

L

P

A

F

S

S

V

V

active site: H168 (= H129), H173 (= H134), E213 (= E175), S232 (= S194)
binding fe (ii) ion: H168 (= H129), H173 (= H134), E213 (= E175)
binding 5,6,7,8-tetrahydrobiopterin: L132 (≠ V93), S134 (≠ D95), F137 (= F98), L138 (≠ F99), A205 (= A167)

1j8tA Catalytic domain of human phenylalanine hydroxylase fe(ii) (see paper)
32% identity, 79% coverage: 27:259/294 of query aligns to 62:295/307 of 1j8tA

query
sites
1j8tA

Y

Y

T

M

Q

E

A

E

E

E

H

K

D

K

V

T

W

W

I

G

T

T

L

V

Y

F

E

K

R

T

Q

L

T

K

D

S

M

L

L

Y

H

K

G

T

R

H

A

A

C

C

D

Y

E

E

F

Y

M

N

R

H

G

I

L

F

D

P

A

L

L

L

D

E

-

K

-

Y

-

C

-

G

L

F

H

H

R

E

S

D

G

N

I

I

P

P

D

Q

F

L

A

E

R

D

I

V

N

S

E

Q

E

F

L

L

K

Q

R

T

L

C

T

T

G

G

W

F

T

R

V

L

V

R

A

P

V

V

P

A

G

G

L

L

V

L

P

S

D

S

D

R

V

D

F

F

F

L

D

G

H

G

L

L

A

A

N

F

R

R

R

V

F

F

P

H

A

C

G

T

Q

Q

F

Y

I

I

R

R

K

H

P

G

H

S

E

K

L

P

D

M

Y

Y

L

T

Q

P

E

E

P

P

D

D

I

I

F

C

H
|
H

D

E

V

L

F

L

G

G

H
|
H

V

V

P

P

M

L

L

F

T

S

D

D

P

R

V

S

F

F

A

A

D

Q

Y

F

M

S

Q

Q

A

-

Y

-

G

-

E

E

G

I

G

G

R

L

R

A

A

S

L

L

G

G

L

A

-

P

-

D

G

E

R

Y

L

I

A

E

N

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

M

C

N

K

T

Q

P

G

A

D

G

S

L

I

R

K

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Y

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S

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-

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V

active site: H168 (= H129), H173 (= H134), E213 (= E175), S232 (= S194)
binding fe (ii) ion: H168 (= H129), H173 (= H134), E213 (= E175)

1dmwA Crystal structure of double truncated human phenylalanine hydroxylase with bound 7,8-dihydro-l-biopterin (see paper)
32% identity, 79% coverage: 27:259/294 of query aligns to 62:295/307 of 1dmwA

query
sites
1dmwA

Y

Y

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A

E

E

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F

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V

active site: H168 (= H129), H173 (= H134), E213 (= E175), S232 (= S194)
binding fe (iii) ion: H168 (= H129), H173 (= H134), E213 (= E175)
binding 7,8-dihydrobiopterin: G130 (= G91), L132 (≠ V93), S134 (≠ D95), F137 (= F98), A205 (= A167), Y208 (= Y170)

4anpA Crystal structure of human phenylalanine hydroxylase in complex with a pharmacological chaperone (see paper)
32% identity, 79% coverage: 27:259/294 of query aligns to 63:296/309 of 4anpA

query
sites
4anpA

Y

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active site: H169 (= H129), H174 (= H134), E214 (= E175), S233 (= S194)
binding 5,6-dimethyl-3-(4-methyl-2-pyridinyl)-2-thioxo-2,3-dihydrothieno[2,3- d]pyrimidin-4(1h)-one: F138 (= F98), P163 (≠ Q123), P165 (= P125), H169 (= H129), W210 (= W171), E214 (= E175)
binding fe (iii) ion: H169 (= H129), H174 (= H134), E214 (= E175)

P00439 Phenylalanine-4-hydroxylase; PAH; Phe-4-monooxygenase; EC 1.14.16.1 from Homo sapiens (Human) (see 43 papers)
32% identity, 79% coverage: 27:259/294 of query aligns to 179:412/452 of P00439

query
sites
P00439

Y

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V

V190 (≠ L38) to A: in PKU; haplotype 3; dbSNP:rs62514919
H201 (≠ R49) to Y: in non-PKU HPA; haplotype 1; dbSNP:rs62517205
Y204 (≠ D52) to C: in PKU; mild; haplotypes 3,4; dbSNP:rs62514927
N207 (≠ M55) to S: in PKU; severe; haplotype 4; dbSNP:rs62508721
P211 (≠ D59) to T: in PKU; haplotype 4; dbSNP:rs62514931
L213 (= L61) to P: in PKU; severe; dbSNP:rs62516109
G218 (vs. gap) to V: in PKU; haplotypes 1,2; dbSNP:rs62514933
E221 (≠ R65) to G: in PKU; haplotype 4; dbSNP:rs62514934
D222 (≠ S66) to V: in PKU; haplotypes 3,4; dbSNP:rs62507319
I224 (= I68) to M: in PKU; haplotype 4; dbSNP:rs199475576
P225 (= P69) to T: in PKU; haplotype 1; dbSNP:rs199475589
V230 (≠ I74) to I: in non-PKU HPA and PKU; haplotype 4; dbSNP:rs62516152
F233 (≠ E77) to L: in PKU; haplotypes 2,3; dbSNP:rs62517208
T238 (= T82) to P: in PKU; haplotype 4; dbSNP:rs199475577
R241 (≠ T85) to C: in non-PKU HPA and PKU; haplotype 34; dbSNP:rs76687508; to H: in PKU; haplotypes 1,5; dbSNP:rs62508730
R243 (≠ V87) to Q: in non-PKU HPA and PKU; haplotypes 4,7,9; dbSNP:rs62508588
P244 (≠ A88) to L: in PKU; haplotype 12; dbSNP:rs118203923
V245 (= V89) to A: in PKU, HPA and non-PKU HPA; haplotypes 3,7; dbSNP:rs796052017; to E: in PKU; haplotype 11; dbSNP:rs76212747
G247 (= G91) to V: in PKU; haplotype 4; dbSNP:rs199475579
L249 (≠ V93) to F: in PKU; haplotype 1; dbSNP:rs74503222
R252 (≠ D96) 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 (≠ F99) to S: in PKU; haplotype 36; dbSNP:rs62642930; to V: in PKU; haplotypes 18,21; dbSNP:rs62642931
A259 (= A103) to T: in PKU; haplotype 3; dbSNP:rs62642932; to V: in PKU; haplotypes 7,42; dbSNP:rs118203921
R261 (= R105) to Q: in HPA and PKU; mild; haplotypes 1,2,4,22, 24,28; dbSNP:rs5030849
I269 (= I113) to L: in non-PKU HPA; dbSNP:rs62508692
R270 (= R114) to S: in PKU; haplotype 1; dbSNP:rs62514951
S273 (≠ H117) to F: in PKU; haplotype 7; dbSNP:rs62514953
P275 (≠ L119) to L: in PKU; reduced activity; increased affinity for the substrate; mildly reduced substrate activation; decreased cofactor affinity; dbSNP:rs62508715
M276 (≠ D120) to V: in PKU; haplotype 4; dbSNP:rs62516149
Y277 (= Y121) to D: in PKU; haplotype 2; dbSNP:rs78655458
E280 (= E124) to K: in PKU; haplotypes 1,2,4,16,38; partial residual activity; dbSNP:rs62508698
P281 (= P125) to L: in PKU; haplotypes 1,4; dbSNP:rs5030851
D282 (= D126) to N: in PKU; haplotype 1; dbSNP:rs199475582
I283 (= I127) 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 (≠ P141) to C: in PKU; haplotype 4; dbSNP:rs62642945
F299 (= F143) to C: in PKU; haplotype 8; dbSNP:rs62642933
A300 (= A144) 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 (≠ M147) to P: in PKU; haplotype 5; dbSNP:rs199475608
I306 (≠ G153) to V: in non-PKU HPA and PKU; haplotype 4; dbSNP:rs62642934
A309 (≠ R156) to D: in PKU; haplotype 7; dbSNP:rs62642935
S310 (≠ A157) 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 (= L158) to P: in PKU; haplotypes 1,7,10; dbSNP:rs62642936
P314 (vs. gap) 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 (≠ L163) to T: in PKU; partial loss of activity; dbSNP:rs62642918
A322 (= A167) to G: in PKU; haplotype 12; dbSNP:rs62514958; to T: in PKU; haplotype 1; dbSNP:rs62514957
F331 (= F176) to L: in PKU; haplotype 1; dbSNP:rs62517179
D338 (≠ A183) to Y: in PKU; haplotype 4; dbSNP:rs62516150
A342 (≠ I187) to T: in PKU; haplotype 5; dbSNP:rs62507282
A345 (= A190) to T: in PKU; haplotype 7; dbSNP:rs62516062
L348 (≠ V193) to V: in PKU; mild haplotype 9; dbSNP:rs62516092
S349 (= S194) to L: in PKU; severe; dbSNP:rs62507279; to P: in PKU; haplotypes 1,4; dbSNP:rs62508646
S350 (= S195) to T: in PKU; haplotype 2; dbSNP:rs62517183
L364 (≠ R210) natural variant: Missing (in PKU; haplotype 5; dbSNP:rs62516096)
Y377 (= Y223) to C: in PKU; haplotype 4; dbSNP:rs62642942
T380 (≠ D226) to M: in non-PKU HPA and PKU; haplotype 4; dbSNP:rs62642937
Y387 (≠ F233) to H: in PKU; haplotype 1; dbSNP:rs62517194
V388 (= V234) to M: in PKU; haplotypes 1,4; dbSNP:rs62516101
E390 (≠ D236) to G: in PKU and non-PKU HPA; haplotype 4; dbSNP:rs5030856
A395 (≠ L241) to P: in PKU; haplotype 1; dbSNP:rs62516103
A403 (≠ G250) to V: in non-PKU HPA and PKU; haplotype 43; dbSNP:rs5030857
R408 (= R255) to Q: in PKU; haplotypes 4,12; dbSNP:rs5030859; to 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
F410 (≠ A257) to S: in PKU; mild; dbSNP:rs62644475

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
176 R → L: in non-PKU HPA and PKU; dbSNP:rs74486803
177 V → L: in PKU; haplotype 6; dbSNP:rs199475602
178 E → G: in non-PKU HPA; dbSNP:rs77958223
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

3e2tA The catalytic domain of chicken tryptophan hydroxylase 1 with bound tryptophan (see paper)
34% identity, 78% coverage: 27:255/294 of query aligns to 63:292/307 of 3e2tA

query
sites
3e2tA

Y

F

T

T

Q

E

A

E

E

E

H

I

D

K

V

T

W

W

I

G

T

T

L

V

Y

Y

E

R

R

E

Q

L

T

N

D

K

M

L

L

Y

H

P

G

T

R

H

A

A

C

C

D

R

E

E

F

Y

M

L

R

K

G

N

L

L

D

P

A

L

L

L

D

T

L

K

H

Y

-

C

-

G

-

Y

-

R

R

E

S

D

G

N

I

I

P

P

D

Q

F

L

A

E

R

D

I

V

N

S

E

R

E

F

L

L

K

K

R

E

L

R

T

T

G

G

W

F

T

T

V

I

V

R

A

P

V

V

P

A

G

G

L

Y

V

L

P

S

D

P

D

R

V

D

F

F

F

L

D

A

H

G

L

L

A

A

N

F

R

R

R

V

F

F

P

H

A

C

G

T

Q

Q

F

Y

I

V

R
|
R

K

H

P

S

H

S

E

D

L

P

D

L

Y
|
Y

L
x
T

Q

P

E
|
E

P
|
P

D

D

I

T

F

C

H
|
H

D

E

V

L

F

L

G

G

H
|
H

V

V

P

P

M

L

L

L

T

A

D

E

P

P

V

S

F

F

A

A

D

Q

Y

F

M

S

Q

Q

A

-

Y

-

G

-

E

E

G

I

G

G

R

L

R

A

A

S

L

L

G

G

L

A

G

S

R

D

L

E

A

A

-

V

-

Q

N

K

L

L

A

A

R

T

L

C

Y

Y

W

F

Y

F

T

T

V

V

E
|
E

F
|
F

G

G

L

L

M

C

N

K

T

Q

P

E

A

G

G

Q

L

L

R

R

I

V

Y

Y

G

G

A

A

G

G

I

L

V

L

S
|
S

S

S

R

I

T

S

E

E

S

L

I

K

F

H

A

S

L

L

D

S

D

G

P

-

S

S

P

A

N

K

R

V

I

K

G

P

F

F

D

D

L

P

E

K

R

V

V

T

M

C

R

K

T

Q

L

E

Y

C

R

L

I
|
I

D

T

F

F

Q

Q

Q

E

V

V

Y

Y

F

F

V

V

I

S

D

E

S

S

I

F

Q

E

T

E

L

A

Q

K

E

E

V

-

T

K

L

M

R

R

D

E

F

F

G

A

A

K

I

T

Y

I

E

K

R

R

active site: H169 (= H129), H174 (= H134), E214 (= E175), S233 (= S194)
binding fe (iii) ion: H169 (= H129), H174 (= H134), E214 (= E175)
binding imidazole: H169 (= H129), H174 (= H134), E214 (= E175)
binding tryptophan: R154 (= R114), Y161 (= Y121), T162 (≠ L122), E164 (= E124), P165 (= P125), H169 (= H129), F215 (= F176), S233 (= S194), I263 (= I225)

Query Sequence

>CCNA_01684 FitnessBrowser__Caulo:CCNA_01684
MSGDGLSNGPPPGARPDWTIDQGWETYTQAEHDVWITLYERQTDMLHGRACDEFMRGLDA
LDLHRSGIPDFARINEELKRLTGWTVVAVPGLVPDDVFFDHLANRRFPAGQFIRKPHELD
YLQEPDIFHDVFGHVPMLTDPVFADYMQAYGEGGRRALGLGRLANLARLYWYTVEFGLMN
TPAGLRIYGAGIVSSRTESIFALDDPSPNRIGFDLERVMRTLYRIDDFQQVYFVIDSIQT
LQEVTLRDFGAIYERLASVSDIGVAEIVPGDAVLTRGTQAYATAGGRLAGAAAG

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