SitesBLAST

N28 (= N29) mutation to A: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
K42 (= K43) 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 (= H169) binding
H218 (= H216) 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 (= Y227) mutation to F: Loss of the epimerase activity.

1jdiA Crystal structure of l-ribulose-5-phosphate 4-epimerase (see paper)
50% identity, 94% coverage: 5:221/231 of query aligns to 4:223/223 of 1jdiA

query
sites
1jdiA

E

D

L

L

K

K

R

R

E

Q

V

V

Y

L

E

E

A

A

N

N

M

L

E

A

L

L

E

P

K

K

R

H

K

N

L

L

V

V

T

T

Y

L

T

T

F

W

G

G

N

N

V

V

S

S

Q

A

I

V

D

D

R

R

Q

E

L

R

G

G

V

V

I

F

G

V

I

I

K

K

P

P

S

S

G

G

V

V

P

D

Y

Y

E

S

D

I

L

M

K

T

V

A

E

D

D

D

I

M

V

V

I

V

V

V

D

S

L

I

E

E

-

T

N

G

Q

E

I

V

V

V

E

E

G

G

R

A

M

K

R

K

P

P

S

S

D
|
D

T

T

K

P

T

T

H

H

T

R

Y

L

L

L

Y

Y

R

Q

Q

A

W

F

Q

P

S

S

I

I

G

G

I

I

T

V

H
|
H

T

T

H
|
H

S

S

T

R

Y

H

A

A

T

T

A

I

W

W

A

A

Q

Q

A

A

Q

G

I

Q

A

S

I

I

P

P

C

A

L

T

G

G

T
|
T

T

T

Q

H

A

A

D
|
D

Y

Y

V

F

Y

Y

G

G

E

T

I

I

P

P

C

C

T

T

A

R

V

K

M

M

R

T

N

D

D

A

Q

E

I

I

S

N

R

G

D

E

Y

Y

E

E

E

W

E

E

T

T

G

G

V

N

Q

V

I

I

L

V

D

E

C

T

F

F

A

E

D

K

R

Q

-

G

-

I

D

D

P

A

N

A

E

Q

S

M

P

P

M

G

V

V

I

L

V

V

A

H

G

S

H
|
H

A

G

P

P

F

F

T

A

W

W

G

G

A

K

N

N

A

A

A

E

K

D

S

A

V

V

Y

H

H

N

A

A

V

I

L

V

L

L

E

E

I

V

A

A

R

Y

M

M

A

G

Y

I

L

F

T

C

K

R

T

Q

L

L

S

A

P

P

G

Q

I

L

S

P

Q

D

L

M

K

Q

Q

Q

E

T

L

L

I

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 (= H169)
binding zinc ion: H95 (= H95), H97 (= H97), H171 (= H169)

6btgA Crystal structure of deoxyribose-phosphate aldolase bound with dhap from bacillus thuringiensis (see paper)
38% identity, 40% coverage: 22:114/231 of query aligns to 22:114/207 of 6btgA

query
sites
6btgA

L

L

V

T

T

K

Y

G

T

T

F

G

G

G

N

N

V

I

S

S

Q

I

I

F

D

N

R

R

Q

E

L

Q

G

G

V

L

I

V

G

A

I

I

K

S

P

P

S

S

G

G

V

L

P

E

Y

Y

E

Y

D

E

L

T

K

K

V

P

E

E

D

D

I

V

V

V

I

I

V

L

D

N

L

L

E

D

N

G

Q

E

I

V

V

I

E

E

G

G

R

E

M

R

R

K

P

P

S

S

D
x
E

T

L

K

D

T

M

H

H

T

L

Y

I

L

Y

Y

Y

R

R

Q

K

W

R

Q

E

S

D

I

I

G

N

G

A

I

L

T

V

H
|
H

T

T

H
|
H

S

S

T

P

Y

Y

A

A

T

K

A

T

W

I

A

A

Q

S

A

L

Q

G

I

W

A

E

I

L

P

P

C

A

L

V

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

Sites not aligning to the query:

active site: 116, 157
binding manganese (ii) ion: 157

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)
38% identity, 40% coverage: 22:114/231 of query aligns to 22:114/213 of P0DTQ0

query
sites
P0DTQ0

L

L

V

T

T

K

Y

G

T

T

F

G

G

G

N

N

V

I

S

S

Q

I

I

F

D

N

R

R

Q

E

L

Q

G

G

V

L

I

V

G

A

I

I

K

S

P

P

S

S

G

G

V

L

P

E

Y

Y

E

Y

D

E

L

T

K

K

V

P

E

E

D

D

I

V

V

V

I

I

V

L

D

N

L

L

E

D

N

G

Q

E

I

V

V

I

E

E

G

G

R

E

M

R

R

K

P

P

S

S

D
x
E

T

L

K

D

T

M

H

H

T

L

Y

I

L

Y

Y

Y

R

R

Q

K

W

R

Q

E

S

D

I

I

G

N

G

A

I

L

T

V

H
|
H

T

T

H
|
H

S

S

T

P

Y

Y

A

A

T

K

A

T

W

I

A

A

Q

S

A

L

Q

G

I

W

A

E

I

L

P

P

C

A

L

V

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

Sites not aligning to the query:

157 binding

4c25A L-fuculose 1-phosphate aldolase (see paper)
34% identity, 48% coverage: 1:112/231 of query aligns to 4:115/212 of 4c25A

query
sites
4c25A

M

M

S

A

F

S

L

S

E

D

L

V

K

K

R

Q

E

E

V

L

Y

I

E

K

A

Y

N

G

M

K

E

K

L

L

E

V

K

E

R

T

K

D

L

L

V

T

T

K

Y

G

T

T

F
x
G

G

G

N

N

V

L

S

S

Q

V

I

F

D

D

R

R

Q

E

L

K

G

Q

V

L

I

M

G

A

I

I

K

T

P

P

S

S

G

G

V

I

P

D

Y

F

E

F

D

E

L

I

K

K

V

E

E

S

D

D

I

I

V

V

I

V

V

M

D

D

L

I

E

N

N

G

Q

N

I

V

V

V

E

E

G

G

R

E

M

R

R

L

P

P

S

S

D
x
E

T

W

K

Y

T

M

H

H

T

L

Y

I

L

Q

Y

Y

R

Q

Q

T

W

R

Q

D

S

D

I

I

G

D

G

A

I

I

T

I

H
|
H

T

A

H
|
H

S

T

T

T

Y

Y

A

A

T

T

A

V

W

L

A

A

Q

C

A

L

Q

R

I

E

A

P

I

L

P

P

active site: E79 (≠ D76), H98 (= H95), H100 (= H97)
binding zinc ion: G30 (≠ F27), H98 (= H95), H100 (= H97)

Sites not aligning to the query:

active site: 119, 160
binding zinc ion: 160

2fuaA L-fuculose 1-phosphate aldolase crystal form t with cobalt (see paper)
31% identity, 54% coverage: 5:128/231 of query aligns to 5:125/210 of 2fuaA

query
sites
2fuaA

E

K

L

L

K

A

R

R

E

Q

V

I

Y

I

E

D

A

T

N

C

M

L

E

E

L

M

E

T

K

R

R

L

K

G

L

L

V

N

T

Q

Y

G

T

T

F

A

G

G

N

N

V

V

S

S

Q

-

I

V

D

R

R

Y

Q

Q

L

D

G

G

V

M

I

L

G

-

I

I

K

T

P

P

S

T

G

G

V

I

P

P

Y

Y

E

E

D

K

L

L

K

T

V

E

E

S

D

H

I

I

V

V

I

F

V

I

D

D

L

G

E

N

N

G

Q

K

I

H

V

E

E

E

G

G

R

K

M

L

R

-

P

P

S

S

D
x
E

T

W

K

R

T

F

H

H

T

M

Y

A

L

A

Y

Y

R

Q

Q

S

W

R

Q

P

S

D

I

A

G

N

G

A

I

V

T

V

H
|
H

T

N

H
|
H

S

A

T

V

Y

H

A

C

T

T

A

A

W

V

A

S

Q

I

A

L

Q

N

I

R

A

S

I

I

P

P

C

A

L

I

G

H

T
x
Y

T

M

Q

I

A

A

D
x
A

Y

A

V

G

Y

G

G

N

E

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

4fuaA L-fuculose-1-phosphate aldolase complex with pgh (see paper)
31% identity, 54% coverage: 5:128/231 of query aligns to 5:125/206 of 4fuaA

query
sites
4fuaA

E

K

L

L

K

A

R

R

E

Q

V

I

Y

I

E

D

A

T

N

C

M

L

E

E

L

M

E

T

K

R

R

L

K

G

L

L

V

N

T

Q

Y

G

T

T

F

A

G
|
G

N
|
N

V

V

S

S

Q

-

I

V

D

R

R

Y

Q

Q

L

D

G

G

V

M

I

L

G

-

I

I

K

T

P

P

S
x
T

G

G

V

I

P

P

Y

Y

E

E

D

K

L

L

K

T

V

E

E

S

D

H

I

I

V

V

I

F

V

I

D

D

L

G

E

N

N

G

Q

K

I

H

V

E

E

E

G

G

R

K

M

L

R

-

P

P

S
|
S

D
x
E

T

W

K

R

T

F

H

H

T

M

Y

A

L

A

Y

Y

R

Q

Q

S

W

R

Q

P

S

D

I

A

G

N

G

A

I

V

T

V

H
|
H

T

N

H
|
H

S

A

T

V

Y

H

A

C

T

T

A

A

W

V

A

S

Q

I

A

L

Q

N

I

R

A

S

I

I

P

P

C

A

L

I

G

H

T
x
Y

T

M

Q

I

A

A

D
x
A

Y

A

V

G

Y

G

G

N

E

S

I

I

P

P

C

C

active site: E73 (≠ D76), H92 (= H95), H94 (= H97), Y113 (≠ T116), A117 (≠ D120)
binding phosphoglycolohydroxamic acid: G28 (= G28), N29 (= N29), T43 (≠ S45), 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

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)
31% identity, 54% coverage: 5:128/231 of query aligns to 5:125/215 of P0AB87

query
sites
P0AB87

E

K

L

L

K

A

R

R

E

Q

V

I

Y

I

E

D

A

T

N

C

M

L

E

E

L

M

E

T

K

R

R

L

K

G

L

L

V

N

T

Q

Y

G

T
|
T

F
x
A

G
|
G

N
|
N

V

V

S

S

Q

-

I

V

D

R

R

Y

Q

Q

L

D

G

G

V

M

I

L

G

-

I

I

K

T

P

P

S
x
T

G
|
G

V

I

P

P

Y

Y

E

E

D

K

L

L

K

T

V

E

E

S

D

H

I

I

V

V

I

F

V

I

D

D

L

G

E

N

N

G

Q

K

I

H

V

E

E

E

G

G

R

K

M

L

R

-

P

P

S
|
S

D
x
E

T

W

K

R

T

F

H

H

T

M

Y

A

L

A

Y

Y

R

Q

Q

S

W

R

Q

P

S

D

I

A

G

N

G

A

I

V

T

V

H
|
H

T

N

H
|
H

S

A

T

V

Y

H

A

C

T

T

A

A

W

V

A

S

Q

I

A

L

Q

N

I

R

A

S

I

I

P

P

C

A

L

I

G

H

T
x
Y

T

M

Q

I

A

A

D

A

Y

A

V

G

Y

G

G

N

E

S

I

I

P

P

C

C

T26 (= T26) mutation to A: Decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
A27 (≠ F27) mutation Missing: Strong decrease of the aldolase activity.
GN 28:29 (= GN 28:29) binding
N29 (= N29) 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 45:46) 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).

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, 85% coverage: 3:198/231 of query aligns to 6:176/181 of Q58813

query
sites
Q58813

F

F

L

I

E

K

L

I

K

C

R

R

E

K

V

L

Y

Y

E

D

A

-

N

-

M

-

E

-

L

-

E

-

K

-

R

R

K

K

L

Y

V

V

T

V

Y

G

T

S

F

G

G

G

N
|
N

V

V

S

S

Q

V

I

-

D

-

R

K

Q

E

L

G

G

D

V

K

I

I

G

Y

I

L

K

T

P

P

S

T

G

G

V

S

P

I

Y

L

E

G

D

F

L

L

K

K

V

E

E

D

D

D

I

I

V

A

I

E

V

M

D

D

L

L

E

D

N

G

Q

N

I

V

V

I

E

K

G

G

R

K

M

-

R

-

P

P

S

T

S

S

D

E

T

K

K

N

T

L

H

H

T

L

Y

M

L

I

Y

Y

R

R

Q

K

W

R

Q

N

S

D

I

I

G

N

G

A

I

I

T

I

H

H

T

T

H

H

S

S

T

L

Y

I

A

S

T

T

A

F

W

L

A

S

Q

T

A

I

Q

N

I

K

A

E

I

I

P

E

C

L

L

L

G

-

T

T

T

P

Q

E

A

G

D

K

Y

I

V

F

Y

L

G

K

E

K

I

I

P

G

C

Y

T

V

A

-

V

-

M

-

R

-

N

-

D

-

Q

-

I

-

S

-

R

-

D

D

Y

Y

E

Y

E

E

E

A

T

G

G

S

V

L

Q

K

I

L

L

A

D

E

C

E

F

T

A

A

D

K

R

R

D

D

P

E

N

D

E

-

S

-

P

-

M

V

V

I

I

I

V

L

A

K

G

N

H

H

A

G

P

V

F

V

T

C

W

L

G

G

A

K

N

D

A

L

A

I

K

D

S

A

V

Y

Y

I

H

K

A

V

V

E

L

V

L

L

E

E

I

Q

A

A

R

K

M

L

A

T

Y

L

L

L

T

N

N25 (= N29) 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.

1dzuP L-fuculose-1-phosphate aldolase from escherichia coli mutant t26a (see paper)
30% identity, 54% coverage: 5:128/231 of query aligns to 5:125/209 of 1dzuP

query
sites
1dzuP

E

K

L

L

K

A

R

R

E

Q

V

I

Y

I

E

D

A

T

N

C

M

L

E

E

L

M

E

T

K

R

R

L

K

G

L

L

V

N

T

Q

Y

G

T

A

F

A

G

G

N

N

V

V

S

S

Q

-

I

V

D

R

R

Y

Q

Q

L

D

G

G

V

M

I

L

G

-

I

I

K

T

P

P

S

T

G

G

V

I

P

P

Y

Y

E

E

D

K

L

L

K

T

V

E

E

S

D

H

I

I

V

V

I

F

V

I

D

D

L

G

E

N

N

G

Q

K

I

H

V

E

E

E

G

G

R

K

M

L

R

-

P

P

S

S

D
x
E

T

W

K

R

T

F

H

H

T

M

Y

A

L

A

Y

Y

R

Q

Q

S

W

R

Q

P

S

D

I

A

G

N

G

A

I

V

T

V

H
|
H

T

N

H
|
H

S

A

T

V

Y

H

A

C

T

T

A

A

W

V

A

S

Q

I

A

L

Q

N

I

R

A

S

I

I

P

P

C

A

L

I

G

H

T

Y

T

M

Q

I

A

A

D

A

Y

A

V

G

Y

G

G

N

E

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)
30% identity, 53% coverage: 6:128/231 of query aligns to 6:122/203 of 7x78A

query
sites
7x78A

L

L

K

A

R
|
R

E

Q

V

I

Y

I

E

D

A

T

N

C

M

L

E

E

L

M

E

T

K

R

R

L

K

G

L

L

V

-

T

-

Y

-

T

N

F

A

G

G

N
|
N

V

V

S

S

Q

V

I

-

D

-

R

R

Q

Y

L

Q

G

G

V

G

I

M

G

L

I

I

K

T

P

P

S
x
T

G

G

V

I

P

P

Y

Y

E

E

D

K

L

L

K

T

V

E

E

D

D

K

I

I

V

V

I

F

V

I

D

D

L

A

E

D

N

G

Q

Q

I
x
H

V

E

E
x
Q

G

G

R

K

M

L

R

-

P

P

S
|
S

D
x
E

T

W

K

R

T

F

H

H

T

Q

Y

A

L

A

Y

Y

R

Q

Q

T

W

R

Q

P

S

D

I

A

G

Q

G

A

I

V

T

V

H
|
H

T

N

H
|
H

S

A

T

V

Y

H

A

C

T

T

A

A

W

V

A

S

Q

I

A

L

Q

N

I

R

A

P

I

I

P

P

C

A

L

I

G

H

T

Y

T

M

Q

I

A

A

D

A

Y

A

V

G

Y

G

G

N

E

S

I

I

P

P

C

C

binding magnesium ion: E70 (≠ D76), H89 (= H95), H91 (= H97)
binding sulfate ion: R8 (= R8), N26 (= N29), T40 (≠ S45), H61 (≠ I66), Q63 (≠ E68), S68 (= S74), S69 (= S75)

Sites not aligning to the query:

6voqA Crystal structure of ygbl, a putative aldolase/epimerase/decarboxylase from klebsiella pneumoniae
24% identity, 85% coverage: 1:196/231 of query aligns to 2:188/207 of 6voqA

query
sites
6voqA

M

M

S

T

F

E

L

Q

E

Q

L

L

K

R

R

E

E

E

V

M

Y

V

E

Q

A

I

N

G

M

A

E

S

L

L

E

F

K

S

R

R

K

G

L

Y

V

A

T

T

Y

G

T

S

F

A

G

G

N

N

V

L

S

S

Q

L

I

L

D

L

R

P

Q

D

L

-

G

G

V

N

I

L

G

L

I

A

K

T

P

P

S

T

G

G

V

A

P

C

Y

L

E

G

D

E

L

L

K

Q

V

A

E

Q

D

R

I

L

V

S

I

V

V

V

D

T

L

L

E

Q

N

G

Q

E

I

W

V

I

E

S

G

G

R

D

M

-

R

K

P

P

S

S

S

K

D
x
E

T

V

K

T

T

F

H

H

T

R

Y

A

L

V

Y

Y

R

L

Q

H

W

N

Q

P

S

A

I

C

G

K

G

A

I

I

T

V

H
|
H

T

L

H
|
H

S

S

T

H

Y

Y

A

L

T

T

A

A

W

L

A

S

Q

C

A

L

Q

Q

I

G

A

L

I

D

P

P

-

H

-

N

C

C

L

I

G

R

T

P

T

F

Q

T

A

P

D
x
Y

Y

V

V

V

Y

M

-

R

-

V

G

G

E

D

I

V

P

P

C

V

T

V

A

P

V

Y

M

Y

R

R

-

P

-

G

N

D

D

D

Q

R

I

I

S

A

R

-

D

-

Y

-

E

-

T

-

G

-

V

-

Q

Q

I

A

L

L

D

A

C

G

F

L

A

A

D

P

R

R

D

-

P

-

N

-

E

-

S

Y

P

N

M

A

V

F

I

L

V

L

A

A

G

N

H
|
H

A

G

P

P

F

V

T

V

W

T

G

G

A

S

N

S

A

L

A

R

K

E

S

A

V

T

Y

N

H

N

A

T

V

E

L

E

L

L

E

E

I

T

A

A

R

R

M

L

A

I

Y

F

active site: E75 (≠ D76), H94 (= H95), H96 (= H97), Y121 (≠ D120), H161 (= H169)
binding zinc ion: E75 (≠ D76), H94 (= H95), H96 (= H97), H161 (= H169)

Query Sequence

>7024891 FitnessBrowser__ANA3:7024891
MSFLELKREVYEANMELEKRKLVTYTFGNVSQIDRQLGVIGIKPSGVPYEDLKVEDIVIV
DLENQIVEGRMRPSSDTKTHTYLYRQWQSIGGITHTHSTYATAWAQAQIAIPCLGTTQAD
YVYGEIPCTAVMRNDQISRDYEEETGVQILDCFADRDPNESPMVIVAGHAPFTWGANAAK
SVYHAVLLEEIARMAYLTKTLSPGISQLKQELIDKHYLRKHGKDAYYGQSK

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