SitesBLAST

N28 (= N28) mutation to A: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
K42 (= K42) mutation to M: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
D76 (= D76) mutation to N: Mutant shows a strong decrease of the catalytic efficiency, but it retains considerable epimerase activity. The affinity for L-ribulose 5-phosphate (LRu5P) is relatively unaffected.
H95 (= H95) binding ; mutation to N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+).
H97 (= H97) binding ; mutation to N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+). Inhibited by glycolaldehyde phosphate.
T116 (= T116) mutation T->E,Y: Loss of the epimerase activity due to an increased steric bulk introduced by the mutation which causes a conformational change that is incompatible with catalysis.
D120 (= D120) mutation to N: Loss of the epimerase activity.
E142 (= E142) mutation to Q: Mutant shows a strong decrease of the catalytic efficiency, but it retains considerable epimerase activity. The affinity for L-ribulose 5-phosphate (LRu5P) is relatively unaffected.
H171 (= H171) binding
H218 (= H218) mutation to N: Mutant shows a strong decrease of the catalytic efficiency, but it retains considerable epimerase activity. The affinity for L-ribulose 5-phosphate (LRu5P) is relatively unaffected.
Y229 (= Y229) mutation to F: Loss of the epimerase activity.

1jdiA Crystal structure of l-ribulose-5-phosphate 4-epimerase (see paper)
75% identity, 97% coverage: 1:223/231 of query aligns to 1:223/223 of 1jdiA

query
sites
1jdiA

M

M

L

L

E

E

Q

D

L

L

K

K

A

R

D

Q

V

V

L

L

A

E

A

A

N

N

L

L

A

A

L

L

P

P

A

K

H

H

H

N

L

L

V

V

T

T

F

L

T

T

W

W

G

G

N

N

V

V

S

S

A

A

V

V

D

D

E

R

T

E

R

R

Q

G

W

V

M

F

V

V

I

I

K

K

P

P

S

S

G

G

V

V

E

D

Y

Y

D

S

V

I

M

M

T

T

A

A

D

D

M

M

V

V

E

S

I

I

A

E

S

T

G

G

K

E

V

V

E

E

G

G

S

A

K

K

P

P

S

S

D
|
D

T

T

P

P

T

T

H

H

L

R

A

L

L

L

Y

Y

R

Q

R

A

Y

F

A

P

E

S

I

I

G

G

I

I

V

V

H
|
H

T

T

H
|
H

S

S

R

R

H

H

A

A

T

T

I

I

W

W

S

A

Q

Q

A

A

G

G

L

Q

D

S

L

I

P

P

A

A

W

T

G

G

T
|
T

T

T

H

H

A

A

D
|
D

Y

Y

F

F

Y

Y

G

G

A

T

I

I

P

P

C

C

T

T

R

R

Q

K

M

M

T

T

A

D

E

A

E

E

I

I

N

N

G

G

E

E

Y

Y

E

E

Y

W

Q

E

T

T

G

G

E

N

V

V

I

I

I

V

E

E

T

T

F

F

E

E

E

K

R

Q

G

G

R

I

S

D

P

A

A

A

Q

Q

I

M

P

P

A

G

V

V

L

L

V

V

H

H

S

S

H
|
H

G

G

P

P

F

F

A

A

W

W

G

G

K

K

N

N

A

A

A

E

D

D

A

A

V

V

H

H

N

N

A

A

V

I

V

V

L

L

E

E

C

V

A

A

Y

Y

M

M

G

G

L

I

F

F

S

C

R

R

Q

Q

L

L

A

A

P

P

Q

Q

L

L

P

P

A

D

M

M

Q

Q

N

Q

E

T

L

L

D

N

K

K

H

H

Y

Y

L

L

R

R

K

K

H

H

active site: D76 (= D76), H95 (= H95), H97 (= H97), T116 (= T116), D120 (= D120), H171 (= H171)
binding zinc ion: H95 (= H95), H97 (= H97), H171 (= H171)

P0DTQ0 5-deoxy-D-ribulose 1-phosphate aldolase; 5-deoxyribose disposal aldolase; EC 4.1.2.- from Bacillus thuringiensis serovar kurstaki (strain ATCC 35866 / NRRL B-4488 / HD73) (see paper)
29% identity, 95% coverage: 1:219/231 of query aligns to 2:207/213 of P0DTQ0

query
sites
P0DTQ0

M

L

L

L

E

Q

Q

K

L

E

K

R

A

E

D

E

V

I

L

V

A

A

A

Y

N

G

L

K

A

K

L

M

P

I

A

S

H

S

H

G

L

L

V

T

T

K

F

G

T

T

W

G

G

G

N

N

V

I

S

S

A

I

V

F

D

N

E

R

T

E

R

Q

Q

G

W

L

M

V

V

A

I

I

K

S

P

P

S

S

G

G

V

L

E

E

Y

Y

D

Y

V

E

M

T

T

K

A

P

D

E

D

D

M

V

V

V

V

I

V

L

E

N

I

L

A

-

S

D

G

G

K

E

V

V

V

I

E

E

G

G

S

E

K

R

K

K

P

P

S

S

D
x
E

T

L

P

D

T

M

H

H

L

L

A

I

L

Y

Y

Y

R

R

R

K

Y

R

A

E

E

D

I

I

G

N

G

A

I

L

V

V

H
|
H

T

T

H
|
H

S

S

R

P

H

Y

A

A

T

K

I

T

W

I

S

A

Q

S

A

L

G

G

L

W

D

E

L

L

P

P

A

A

W

-

G

-

T

V

T

S

H

Y

A

L

D

I

Y

A

F

F

Y

A

G

G

A

-

I

-

P

P

C

N

T

V

R

R

Q

C

M

A

T

P

A

Y

E

E

E

T

I

F

N

G

G

T

E

K

Y

-

E

-

Y

-

Q

Q

T

L

G

A

E

D

V

A

I

A

I

F

E

E

T

G

F

M

E

I

E

D

R

R

G

-

R

-

S

-

P

-

A

-

Q

-

I

-

P

R

A

A

V

V

L

L

V

L

H

A

S

N

H
|
H

G

G

P

L

F

I

A

A

W

G

G

A

K

N

N

N

A

I

A

K

D

M

A

A

V

F

H

T

N

V

A

A

V

E

L

I

E

E

E

F

C

C

A

A

Y

Q

M

I

G

Y

L

Y

F

Q

S

T

R

K

Q

S

L

I

A

G

-

E

P

P

Q

K

-

L

L

L

P

P

A

E

M

D

Q

E

N

M

E

E

L

N

L

L

D

A

K

K

H

K

Y

F

E76 (≠ D76) binding
H95 (= H95) binding
H97 (= H97) binding
H157 (= H171) binding

6btgA Crystal structure of deoxyribose-phosphate aldolase bound with dhap from bacillus thuringiensis (see paper)
29% identity, 95% coverage: 1:219/231 of query aligns to 2:207/207 of 6btgA

query
sites
6btgA

M

L

L

L

E

Q

Q

K

L

E

K

R

A

E

D

E

V

I

L

V

A

A

A

Y

N

G

L

K

A

K

L

M

P

I

A

S

H

S

H

G

L

L

V

T

T

K

F

G

T

T

W

G

G

G

N

N

V

I

S

S

A

I

V

F

D

N

E

R

T

E

R

Q

Q

G

W

L

M

V

V

A

I

I

K

S

P

P

S

S

G

G

V

L

E

E

Y

Y

D

Y

V

E

M

T

T

K

A

P

D

E

D

D

M

V

V

V

V

I

V

L

E

N

I

L

A

-

S

D

G

G

K

E

V

V

V

I

E

E

G

G

S

E

K

R

K

K

P

P

S

S

D
x
E

T

L

P

D

T

M

H

H

L

L

A

I

L

Y

Y

Y

R

R

R

K

Y

R

A

E

E

D

I

I

G

N

G

A

I

L

V

V

H
|
H

T

T

H
|
H

S

S

R

P

H

Y

A

A

T

K

I

T

W

I

S

A

Q

S

A

L

G

G

L

W

D

E

L

L

P

P

A

A

W

-

G

-

T

V

T

S

H
x
Y

A

L

D

I

Y

A

F

F

Y

A

G

G

A

-

I

-

P

P

C

N

T

V

R

R

Q

C

M

A

T

P

A

Y

E

E

E

T

I

F

N

G

G

T

E

K

Y

-

E

-

Y

-

Q

Q

T

L

G

A

E

D

V

A

I

A

I

F

E

E

T

G

F

M

E

I

E

D

R

R

G

-

R

-

S

-

P

-

A

-

Q

-

I

-

P

R

A

A

V

V

L

L

V

L

H

A

S

N

H
|
H

G

G

P

L

F

I

A

A

W

G

G

A

K

N

N

N

A

I

A

K

D

M

A

A

V

F

H

T

N

V

A

A

V

E

L

I

E

E

E

F

C

C

A

A

Y

Q

M

I

G

Y

L

Y

F

Q

S

T

R

K

Q

S

L

I

A

G

-

E

P

P

Q

K

-

L

L

L

P

P

A

E

M

D

Q

E

N

M

E

E

L

N

L

L

D

A

K

K

H

K

Y

F

active site: E76 (≠ D76), H95 (= H95), H97 (= H97), Y116 (≠ H118), H157 (= H171)
binding manganese (ii) ion: E76 (≠ D76), H95 (= H95), H97 (= H97), H157 (= H171)

4c25A L-fuculose 1-phosphate aldolase (see paper)
28% identity, 93% coverage: 5:219/231 of query aligns to 9:210/212 of 4c25A

query
sites
4c25A

L

V

K

K

A

Q

D

E

V

L

L

I

A

K

A

Y

N

G

L

K

A

K

L

L

P

V

A

E

H

T

H

D

L

L

V

T

T

K

F

G

T

T

W
x
G

G

G

N

N

V

L

S

S

A

V

V

F

D

D

E

R

T

E

R

K

Q

Q

W

L

M

M

V

A

I

I

K

T

P

P

S

S

G

G

V

I

E

D

Y

F

D

F

V

E

M

I

T

K

A

E

D

S

D

D

M

I

V

V

V

M

E

D

I

I

A

-

S

N

G

G

K

N

V

V

E

E

G

G

S

E

K

R

K

L

P

P

S

S

D
x
E

T

W

P

Y

T

M

H

H

L

L

A

I

L

Q

Y

Y

R

Q

R

T

Y

R

A

D

E

D

I

I

G

D

G

A

I

I

V

I

H
|
H

T

A

H
|
H

S

T

R

T

H

Y

A

A

T

T

I

V

W

L

S

A

Q

C

A

L

G

R

L

E

D

P

L

L

P

P

A

-

W

-

G

-

T

-

H

-

A

A

D

S

Y

H

F
x
Y

Y

M

G

I

A

A

I

V

P

A

C

G

T

K

R

D

Q

V

M

R

T

V

A

A

E

E

E

Y

I

A

N

T

G

-

E

-

Y

-

E

-

Y

Y

Q

G

T

T

G

K

E

E

V

L

I

A

I

V

E

N

T

A

F

A

E

K

E

A

-

M

R

E

G

G

R

R

S

R

P

-

A

-

Q

-

I

-

P

-

A

A

V

V

L

L

V

L

H

A

S

N

H
|
H

G

G

P

I

F

L

A

A

W

G

G

A

K

Q

N

N

A

L

D

N

A

A

V

F

H

N

N

I

A

V

V

E

L

V

E

E

E

Y

C

C

A

A

Y

K

M

I

G

Y

L

C

F

L

S

A

R

K

Q

N

L

F

A

G

P

E

Q

P

-

V

L

L

P

P

A

D

M

E

Q

E

N

M

E

E

L

L

L

M

D

A

K

E

H

K

Y

F

active site: E79 (≠ D76), H98 (= H95), H100 (= H97), Y119 (≠ F122), H160 (= H171)
binding zinc ion: G30 (≠ W26), H98 (= H95), H100 (= H97), H160 (= H171)

Q58813 L-fuculose phosphate aldolase; L-fuculose-1-phosphate aldolase; EC 4.1.2.17 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
26% identity, 77% coverage: 22:200/231 of query aligns to 19:176/181 of Q58813

query
sites
Q58813

V

V

T

V

F

G

T

S

W

G

G

G

N
|
N

V

V

S

S

A

V

V

K

D

E

E

G

T

D

R

K

Q

I

W

Y

M

L

V

T

I

-

K

-

P

P

S

T

G

G

V

S

E

I

Y

L

D

G

V

F

M

L

T

K

A

E

D

D

M

I

V

A

V

E

V

M

E

D

I

L

A

-

S

D

G

G

K

N

V

V

V

I

E

K

G

G

S

-

K

-

K

K

P

P

S

T

S

S

D

E

T

K

P

N

T

L

H

H

L

L

A

M

L

I

Y

Y

R

R

R

K

Y

R

A

N

E

D

I

I

G

N

G

A

I

I

V

I

H

H

T

T

H

H

S

S

R

L

H

I

A

S

T

T

I

F

W

L

S

S

Q

T

A

I

G

N

L

K

D

E

L

I

P

E

A

L

W

L

G

-

T

T

T

P

H

E

A

G

D

K

Y

I

F

F

Y

L

G

K

A

K

I

I

P

G

C

Y

T

V

R

-

Q

-

M

-

T

-

A

-

E

-

I

-

N

-

G

-

E

D

Y

Y

E

-

Y

Y

Q

E

T

A

G

G

E

S

V

-

I

-

I

L

E

K

T

L

F

A

E

E

R

T

G

A

R

K

S

R

P

D

A

E

Q

D

I

V

P

-

A

-

V

I

L

I

V

L

H

K

S

N

H

H

G

G

P

V

F

V

A

C

W

L

G

G

K

K

N

D

A

L

A

I

D

D

A

A

V

Y

H

I

N

K

A

V

V

E

V

V

L

L

E

E

C

Q

A

A

Y

K

M

L

G

T

L

L

F

L

S

N

N25 (= N28) mutation to L: It shows a 3-fold increase of the affinty for dihydroxyacetone phosphate (DHAP) and a 3-fold decrease of the affinity for DL-glyceraldehyde compared to the wild-type.; mutation to T: It shows a 5-fold decrease of the affinty for dihydroxyacetone phosphate (DHAP), but has the same affinity for DL-glyceraldehyde compared to the wild-type.

4fuaA L-fuculose-1-phosphate aldolase complex with pgh (see paper)
34% identity, 45% coverage: 25:128/231 of query aligns to 26:125/206 of 4fuaA

query
sites
4fuaA

T

T

W

A

G
|
G

N
|
N

V

V

S

S

A

V

V

-

D

-

E

R

T

Y

R

Q

Q

D

W

G

M

M

V

L

I

I

K

T

P

P

S
x
T

G

G

V

I

E

P

Y

Y

D

E

V

K

M

L

T

T

A

E

D

S

D

H

M

I

V

V

V

F

V

I

E

D

I

-

A

G

S

N

G

G

K

K

V

H

V

E

E

E

G

G

S

-

K

K

K

L

P

P

S
|
S

D
x
E

T

W

P

R

T

F

H

H

L

M

A

A

L

A

Y

Y

R

Q

R

S

Y

R

A

P

E

D

I

A

G

N

G

A

I

V

V

V

H
|
H

T

N

H
|
H

S

A

R

V

H

H

A

C

T

T

I

A

W

V

S

S

Q

I

A

L

G

N

L

R

D

S

L

I

P

P

A

A

W

I

G

H

T
x
Y

T

M

H

I

A

A

D
x
A

Y

A

F

G

Y

G

G

N

A

S

I

I

P

P

C

C

active site: E73 (≠ D76), H92 (= H95), H94 (= H97), Y113 (≠ T116), A117 (≠ D120)
binding phosphoglycolohydroxamic acid: G28 (= G27), N29 (= N28), T43 (≠ S44), S71 (= S74), S72 (= S75), E73 (≠ D76), H92 (= H95), H94 (= H97)
binding zinc ion: H92 (= H95), H94 (= H97)

Sites not aligning to the query:

active site: 155
binding phosphoglycolohydroxamic acid: 155
binding zinc ion: 155

2fuaA L-fuculose 1-phosphate aldolase crystal form t with cobalt (see paper)
34% identity, 45% coverage: 25:128/231 of query aligns to 26:125/210 of 2fuaA

query
sites
2fuaA

T

T

W

A

G

G

N

N

V

V

S

S

A

V

V

-

D

-

E

R

T

Y

R

Q

Q

D

W

G

M

M

V

L

I

I

K

T

P

P

S

T

G

G

V

I

E

P

Y

Y

D

E

V

K

M

L

T

T

A

E

D

S

D

H

M

I

V

V

V

F

V

I

E

D

I

-

A

G

S

N

G

G

K

K

V

H

V

E

E

E

G

G

S

-

K

K

K

L

P

P

S

S

D
x
E

T

W

P

R

T

F

H

H

L

M

A

A

L

A

Y

Y

R

Q

R

S

Y

R

A

P

E

D

I

A

G

N

G

A

I

V

V

V

H
|
H

T

N

H
|
H

S

A

R

V

H

H

A

C

T

T

I

A

W

V

S

S

Q

I

A

L

G

N

L

R

D

S

L

I

P

P

A

A

W

I

G

H

T
x
Y

T

M

H

I

A

A

D
x
A

Y

A

F

G

Y

G

G

N

A

S

I

I

P

P

C

C

active site: E73 (≠ D76), H92 (= H95), H94 (= H97), Y113 (≠ T116), A117 (≠ D120)
binding cobalt (ii) ion: E73 (≠ D76), H92 (= H95), H94 (= H97)

Sites not aligning to the query:

active site: 155, 209
binding cobalt (ii) ion: 155

P0AB87 L-fuculose phosphate aldolase; D-ribulose-phosphate aldolase; L-fuculose-1-phosphate aldolase; EC 4.1.2.17 from Escherichia coli (strain K12) (see 4 papers)
34% identity, 45% coverage: 25:128/231 of query aligns to 26:125/215 of P0AB87

query
sites
P0AB87

T
|
T

W
x
A

G
|
G

N
|
N

V

V

S

S

A

V

V

-

D

-

E

R

T

Y

R

Q

Q

D

W

G

M

M

V

L

I

I

K

T

P

P

S
x
T

G
|
G

V

I

E

P

Y

Y

D

E

V

K

M

L

T

T

A

E

D

S

D

H

M

I

V

V

V

F

V

I

E

D

I

-

A

G

S

N

G

G

K

K

V

H

V

E

E

E

G

G

S

-

K

K

K

L

P

P

S
|
S

D
x
E

T

W

P

R

T

F

H

H

L

M

A

A

L

A

Y

Y

R

Q

R

S

Y

R

A

P

E

D

I

A

G

N

G

A

I

V

V

V

H
|
H

T

N

H
|
H

S

A

R

V

H

H

A

C

T

T

I

A

W

V

S

S

Q

I

A

L

G

N

L

R

D

S

L

I

P

P

A

A

W

I

G

H

T
x
Y

T

M

H

I

A

A

D

A

Y

A

F

G

Y

G

G

N

A

S

I

I

P

P

C

C

T26 (= T25) mutation to A: Decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
A27 (≠ W26) mutation Missing: Strong decrease of the aldolase activity.
GN 28:29 (= GN 27:28) binding
N29 (= N28) mutation to L: Loss of aldolase activity; when associated with A-71.; mutation to Q: Strong decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
TG 43:44 (≠ SG 44:45) binding
S71 (= S74) mutation to A: Loss of aldolase activity; when associated with L-29.; mutation to Q: Loss of aldolase activity.
SS 71:72 (= SS 74:75) binding
E73 (≠ D76) active site, Proton donor/acceptor; binding ; mutation to Q: Loss of aldolase activity; when associated with F-113 and F-209.; mutation to S: Loss of aldolase activity.
H92 (= H95) binding
H94 (= H97) binding
Y113 (≠ T116) Plays a key role in the stabilization of the transition state and positioning the aldehyde component; mutation to F: Slowly inactivated. Has a preference for the D-aldehyde and shows an inversion of the diastereoselectivity. Loss of aldolase activity; when associated with Q-73 and F-209.

Sites not aligning to the query:

131 Plays a key role in the stabilization of the transition state and positioning the aldehyde component; F→A: Has a slight preference for the D-aldehyde and shows an inversion of the diastereoselectivity. Loss of aldolase activity; when associated with W-206.
155 binding
206 F→W: Decrease of aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P). Loss of aldolase activity; when associated with A-131.
207:215 mutation Missing: Loss of aldolase activity. Has a slight preference for the D-aldehyde.
209 Plays a key role in the stabilization of the transition state and positioning the aldehyde component; Y→F: Slowly inactivated and unable to discriminate between the enantiomers. Shows an inversion of the diastereoselectivity. Loss of aldolase activity; when associated with Q-73 and F-113.
211:215 mutation Missing: Decrease of aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).

1dzuP L-fuculose-1-phosphate aldolase from escherichia coli mutant t26a (see paper)
33% identity, 44% coverage: 27:128/231 of query aligns to 28:125/209 of 1dzuP

query
sites
1dzuP

G

G

N

N

V

V

S

S

A

V

V

-

D

-

E

R

T

Y

R

Q

Q

D

W

G

M

M

V

L

I

I

K

T

P

P

S

T

G

G

V

I

E

P

Y

Y

D

E

V

K

M

L

T

T

A

E

D

S

D

H

M

I

V

V

V

F

V

I

E

D

I

-

A

G

S

N

G

G

K

K

V

H

V

E

E

E

G

G

S

-

K

K

K

L

P

P

S

S

D
x
E

T

W

P

R

T

F

H

H

L

M

A

A

L

A

Y

Y

R

Q

R

S

Y

R

A

P

E

D

I

A

G

N

G

A

I

V

V

V

H
|
H

T

N

H
|
H

S

A

R

V

H

H

A

C

T

T

I

A

W

V

S

S

Q

I

A

L

G

N

L

R

D

S

L

I

P

P

A

A

W

I

G

H

T

Y

T

M

H

I

A

A

D

A

Y

A

F

G

Y

G

G

N

A

S

I

I

P

P

C

C

binding zinc ion: E73 (≠ D76), H92 (= H95), H94 (= H97)

Sites not aligning to the query:

binding zinc ion: 155

7x78A L-fuculose 1-phosphate aldolase (see paper)
33% identity, 44% coverage: 27:128/231 of query aligns to 25:122/203 of 7x78A

query
sites
7x78A

G

G

N
|
N

V

V

S

S

A

V

V

-

D

-

E

R

T

Y

R

Q

Q

G

W

G

M

M

V

L

I

I

K

T

P

P

S
x
T

G

G

V

I

E

P

Y

Y

D

E

V

K

M

L

T

T

A

E

D

D

D

K

M

I

V

V

V

F

V

I

E

D

I

-

A

A

S

D

G

G

K

Q

V
x
H

V

E

E
x
Q

G

G

S

-

K

K

K

L

P

P

S
|
S

D
x
E

T

W

P

R

T

F

H

H

L

Q

A

A

L

A

Y

Y

R

Q

R

T

Y

R

A

P

E

D

I

A

G

Q

G

A

I

V

V

V

H
|
H

T

N

H
|
H

S

A

R

V

H

H

A

C

T

T

I

A

W

V

S

S

Q

I

A

L

G

N

L

R

D

P

L

I

P

P

A

A

W

I

G

H

T

Y

T

M

H

I

A

A

D

A

Y

A

F

G

Y

G

G

N

A

S

I

I

P

P

C

C

binding magnesium ion: E70 (≠ D76), H89 (= H95), H91 (= H97)
binding sulfate ion: N26 (= N28), T40 (≠ S44), H61 (≠ V66), Q63 (≠ E68), S68 (= S74), S69 (= S75)

Sites not aligning to the query:

Query Sequence

>17644 FitnessBrowser__Keio:17644
MLEQLKADVLAANLALPAHHLVTFTWGNVSAVDETRQWMVIKPSGVEYDVMTADDMVVVE
IASGKVVEGSKKPSSDTPTHLALYRRYAEIGGIVHTHSRHATIWSQAGLDLPAWGTTHAD
YFYGAIPCTRQMTAEEINGEYEYQTGEVIIETFEERGRSPAQIPAVLVHSHGPFAWGKNA
ADAVHNAVVLEECAYMGLFSRQLAPQLPAMQNELLDKHYLRKHGANAYYGQ

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