SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing Dsui_3380 FitnessBrowser__PS:Dsui_3380 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 15 hits to proteins with known functional sites (download)

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)
42% identity, 96% coverage: 7:213/216 of query aligns to 8:210/215 of P0AB87

query
sites
P0AB87

Q

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G

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 (= A26) 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 (= TG 46:47) binding
S71 (= S75) mutation to A: Loss of aldolase activity; when associated with L-29.; mutation to Q: Loss of aldolase activity.
SS 71:72 (= SS 75:76) binding
E73 (= E77) 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 (= H96) binding
H94 (= H98) binding
Y113 (= Y117) 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.
F131 (= F135) Plays a key role in the stabilization of the transition state and positioning the aldehyde component; mutation to 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.
H155 (= H159) binding
F206 (= F209) mutation to 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.
Y209 (= Y212) Plays a key role in the stabilization of the transition state and positioning the aldehyde component; mutation to 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.

Sites not aligning to the query:

207:215 mutation Missing: Loss of aldolase activity. Has a slight preference for the D-aldehyde.
211:215 mutation Missing: Decrease of aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).

2fuaA L-fuculose 1-phosphate aldolase crystal form t with cobalt (see paper)
42% identity, 96% coverage: 7:213/216 of query aligns to 8:210/210 of 2fuaA

query
sites
2fuaA

Q

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active site: E73 (= E77), H92 (= H96), H94 (= H98), Y113 (= Y117), A117 (≠ R121), H155 (= H159), Y209 (= Y212)
binding cobalt (ii) ion: E73 (= E77), H92 (= H96), H94 (= H98), H155 (= H159)

1dzuP L-fuculose-1-phosphate aldolase from escherichia coli mutant t26a (see paper)
41% identity, 95% coverage: 7:212/216 of query aligns to 8:209/209 of 1dzuP

query
sites
1dzuP

Q

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binding zinc ion: E73 (= E77), H92 (= H96), H94 (= H98), H155 (= H159)

4fuaA L-fuculose-1-phosphate aldolase complex with pgh (see paper)
41% identity, 94% coverage: 7:209/216 of query aligns to 8:206/206 of 4fuaA

query
sites
4fuaA

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active site: E73 (= E77), H92 (= H96), H94 (= H98), Y113 (= Y117), A117 (≠ R121), H155 (= H159)
binding phosphoglycolohydroxamic acid: G28 (= G27), N29 (= N28), T43 (= T46), S71 (= S75), S72 (= S76), E73 (= E77), H92 (= H96), H94 (= H98), H155 (= H159)
binding zinc ion: H92 (= H96), H94 (= H98), H155 (= H159)

7x78A L-fuculose 1-phosphate aldolase (see paper)
41% identity, 94% coverage: 7:209/216 of query aligns to 8:203/203 of 7x78A

query
sites
7x78A

Q
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F

binding magnesium ion: E70 (= E77), H89 (= H96), H91 (= H98), H152 (= H159)
binding sulfate ion: R8 (≠ Q7), N26 (= N28), T40 (= T46), H61 (= H68), Q63 (≠ G70), S68 (= S75), S69 (= S76)

Sites not aligning to the query:

binding sulfate ion: 5

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)
34% identity, 97% coverage: 6:215/216 of query aligns to 7:213/213 of P0DTQ0

query
sites
P0DTQ0

R

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E

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V

I

-

E

G

G

R

E

R

R

L

K

P

P

S

S

E
|
E

W

L

R

D

F

M

H

H

R

L

D

I

I

Y

Y

Y

A

R

A

K

R

R

P

E

E

D

T

I

G

N

A

A

V

L

L

V

H
|
H

A

T

H
|
H

S

S

P

P

F

Y

A

A

T

K

S

T

L

I

A

A

C

S

L

L

R

G

R

W

D

E

I

L

P

P

P

A

F

V

H

S

Y

Y

M

L

I

I

A

A

R

-

F

F

G

A

G

G

D

P

T

N

V

V

R

R

C

C

S

A

D

P

Y

Y

A

E

T

T

F

F

G

G

T

T

Q

K

A

Q

L

L

S

A

D

D

T

A

A

A

L

F

A

E

A

G

L

M

E

I

E

D

R

R

K

R

G

A

C

V

L

L

A

A

N

N

H
|
H

G

G

M

L

I

I

V

A

C

G

G

A

K

N

D

N

L

I

G

K

E

M

A

A

L

F

A

T

L

V

G

A

V

E

E

E

L

I

E

E

S

F

L

C

S

A

E

Q

Q

I

F

Y

W

Y

R

Q

A

T

S

K

Q

S

L

I

G

G

S

E

A

P

V

K

L

L

D

P

T

E

E

D

Q

E

M

M

A

E

E

N

A

L

L

A

A

K

R

K

F

F

A

E

T

G

Y

Y

G

G

K

Q

Q

Q

E76 (= E77) binding
H95 (= H96) binding
H97 (= H98) binding
H157 (= H159) binding

4c25A L-fuculose 1-phosphate aldolase (see paper)
36% identity, 96% coverage: 3:209/216 of query aligns to 7:210/212 of 4c25A

query
sites
4c25A

A

S

D

D

P

V

R

K

Q

Q

S

E

L

L

I

I

T

K

A

Y

A

G

H

K

R

K

M

L

A

V

A

E

E

T

G

D

L

L

N

T

R

K

G

G

T

T

A
x
G

G

G

N

N

L

L

S

S

L

V

R

F

A

D

K

R

L

E

D

K

G

Q

V

L

D

-

G

-

F

M

Y

A

V

I

T

T

P

P

T

S

G

G

M

I

N

D

Y

F

D

F

S

E

L

I

Q

K

A

E

E

S

D

D

I

I

P

V

F

V

V

M

K

D

L

I

A

N

D

G

G

N

S

V

H

V

V

E

G

G

R

E

R

R

L

L

P

P

S

S

E
|
E

W

W

R

Y

F

M

H

H

R

L

D

I

I

Q

Y

Y

A

Q

A

T

R

R

P

D

E

D

T

I

G

D

A

A

V

I

L

I

H
|
H

A

A

H
|
H

S

T

P

T

F

Y

A

A

T

T

S

V

L

L

A

A

C

C

L

L

R

R

R

E

D

P

I

L

P

P

P

A

F

S

H

H

Y
|
Y

M

M

I

I

A

A

R

V

F

A

G

G

G

K

D

D

T

-

V

V

R

R

C

V

S

A

D

E

Y

Y

A

A

T

T

F

Y

G

G

T

T

Q

K

A

E

L

L

S

A

D

V

T

N

A

A

L

A

A

K

A

A

L

M

E

E

E

G

R

R

K

R

G

A

C

V

L

L

A

A

N

N

H
|
H

G

G

M

I

I

L

V

A

C

G

G

A

K

Q

D

N

L

L

G

L

E

N

A

A

L

F

A

N

L

I

G

V

V

E

E

E

L

V

E

E

S

Y

L

C

S

A

E

K

Q

I

F

Y

W

C

R

L

A

A

S

K

Q

N

L

F

G

G

S

E

A

P

V

V

L

V

L

L

D

P

T

D

E

E

Q

E

M

M

A

E

E

L

A

M

L

A

A

E

R

K

F

F

active site: E79 (= E77), H98 (= H96), H100 (= H98), Y119 (= Y117), H160 (= H159)
binding zinc ion: G30 (≠ A26), H98 (= H96), H100 (= H98), H160 (= H159)

6btgA Crystal structure of deoxyribose-phosphate aldolase bound with dhap from bacillus thuringiensis (see paper)
33% identity, 94% coverage: 6:209/216 of query aligns to 7:207/207 of 6btgA

query
sites
6btgA

R

R

Q

E

S

E

L

I

I

V

T

A

A

Y

A

G

H

K

R

K

M

M

A

I

A

S

E

S

G

G

L

L

N

T

R

K

G

G

T

T

A

G

G

G

N

N

L

I

S

S

L

I

R

F

A

N

K

R

L

E

D

Q

G

G

V

L

D

V

G

A

F

-

Y

-

V

I

T

S

P

P

T

S

G

G

M

L

N

E

Y

Y

D

Y

S

E

L

T

Q

K

A

P

E

E

D

D

I

V

P

V

F

I

V

L

K

N

L

L

A

-

D

D

G

G

S

E

H

V

V

I

-

E

G

G

R

E

R

R

L

K

P

P

S

S

E
|
E

W

L

R

D

F

M

H

H

R

L

D

I

I

Y

Y

Y

A

R

A

K

R

R

P

E

E

D

T

I

G

N

A

A

V

L

L

V

H
|
H

A

T

H
|
H

S

S

P

P

F

Y

A

A

T

K

S

T

L

I

A

A

C

S

L

L

R

G

R

W

D

E

I

L

P

P

P

A

F

V

H

S

Y
|
Y

M

L

I

I

A

A

R

-

F

F

G

A

G

G

D

P

T

N

V

V

R

R

C

C

S

A

D

P

Y

Y

A

E

T

T

F

F

G

G

T

T

Q

K

A

Q

L

L

S

A

D

D

T

A

A

A

L

F

A

E

A

G

L

M

E

I

E

D

R

R

K

R

G

A

C

V

L

L

A

A

N

N

H
|
H

G

G

M

L

I

I

V

A

C

G

G

A

K

N

D

N

L

I

G

K

E

M

A

A

L

F

A

T

L

V

G

A

V

E

E

E

L

I

E

E

S

F

L

C

S

A

E

Q

Q

I

F

Y

W

Y

R

Q

A

T

S

K

Q

S

L

I

G

G

S

E

A

P

V

K

L

L

D

P

T

E

E

D

Q

E

M

M

A

E

E

N

A

L

L

A

A

K

R

K

F

F

active site: E76 (= E77), H95 (= H96), H97 (= H98), Y116 (= Y117), H157 (= H159)
binding manganese (ii) ion: E76 (= E77), H95 (= H96), H97 (= H98), H157 (= H159)

6voqA Crystal structure of ygbl, a putative aldolase/epimerase/decarboxylase from klebsiella pneumoniae
36% identity, 81% coverage: 6:179/216 of query aligns to 8:181/207 of 6voqA

query
sites
6voqA

R

R

Q

E

S

E

L

M

I

V

T

Q

A

I

A

G

H

A

R

S

M

L

A

F

A

S

E

R

G

G

L

Y

N

A

R

T

G

G

T

S

A

A

G

G

N

N

L

L

S

S

L

L

R

L

A

L

K

P

L

-

D

D

G

G

V

-

D

-

G

N

F

L

Y

L

V

A

T

T

P

P

T

T

G

G

M

A

N

C

Y

L

D

G

S

E

L

L

Q

Q

A

A

E

Q

D

R

I

L

P

S

F

V

V

V

K

T

L

L

A

-

D

Q

G

G

S

E

H

W

V

I

G

S

R

G

R

D

L

K

P

P

S

S

S

K

E
|
E

W

V

R

T

F

F

H

H

R

R

D

A

I

V

Y

Y

A

L

A

H

R

N

P

P

E

A

T

C

G

K

A

A

V

I

L

V

H
|
H

A

L

H
|
H

S

S

P

H

F

Y

A

L

T

T

S

A

L

L

A

S

C

C

L

L

R

Q

-

G

-

L

-

D

-

P

-

H

R

N

D

C

I

I

P

R

P

P

F

F

H

T

-

P

Y
|
Y

M

V

I

V

A

M

R

R

F

V

G

G

G

-

D

-

T

D

V

V

R

P

C

V

S

V

D

P

Y

Y

A

Y

T

R

F

P

G

G

T

D

Q

D

A

R

L

I

S

A

D

Q

T

-

A

A

L

L

A

A

A

G

L

L

E

A

E

P

R

R

-

Y

K

N

G

A

C

F

L

L

A

A

N

N

H
|
H

G

G

M

P

I

V

V

V

C

T

G

G

K

S

D

S

L

L

G

R

E

E

A

A

L

T

A

N

L

N

G

T

V

E

E

E

L

L

E

E

active site: E75 (= E77), H94 (= H96), H96 (= H98), Y121 (= Y117), H161 (= H159)
binding zinc ion: E75 (= E77), H94 (= H96), H96 (= H98), H161 (= H159)

4xxfA L-fuculose 1-phosphate aldolase from glaciozyma antarctica pi12 (see paper)
26% identity, 92% coverage: 6:203/216 of query aligns to 23:216/249 of 4xxfA

query
sites
4xxfA

R

K

Q

E

S

R

L

L

I

V

T

A

A

A

A

I

H

R

R

I

M

F

A

A

A

N

E

E

G

G

L

F

N

D

R

H

G

T

T

V

A

A

G

G

N

H

L

L

S

T

L

V

R

R

A

D

K

P

L

-

D

E

G

N

V

K

D

H

G

H

F

F

Y

W

V

V

T

N

P

P

T

F

G

G

M

L

N

A

Y

F

D

R

S

L

L

M

Q

T

A

V

E

S

D

D

I

L

P

I

F

L

V

V

K

N

-

Q

-

E

-

G

-

T

L

V

A

I

D

G

G

G

S

G

H

K

V

E

G

G

R

R

L

I

P

V

S

N

-

L

S

A

E
x
G

W

F

R

M

F

I

H

H

R

S

D

A

I

I

Y

H

A

K

A

A

R

R

P

P

E

E

T

V

G

Q

A

A

V

I

L

C

H
|
H

A

S

H
|
H

S

S

P

T

F

Y

A

G

T

K

S

A

L

F

A

S

C

S

L

L

R

G

R

K

D

P

I

L

P

A

P

I

F

T

H

T

Y
x
Q

M

D

I

S

A

C

R

A

F

F

G

Y

G

G

D

D

T

V

V

A

R

L

C

L

S

G

D

D

Y

E

A

-

T

-

F

-

G

-

T

-

Q

-

A

-

L

-

S

S

D

G

T

T

A

I

L

A

A

V

A

A

L

L

E

Q

R

K

K

K

G

A

C

I

L

I

L

L

A

Q

N

N

H
|
H

G

G

M

L

I

L

V

T

C

V

G

G

K

T

D

T

L

I

G

D

E

S

A

A

L

V

A

A

L

W

G

F

V

I

E

M

L

L

E

E

S

K

L

Q

S

C

E

Q

Q

V

F

Q

W

L

R

L

A

A

S

D

Q

A

L

A

G

G

S

Q

A

T

V

I

L

P

L

I

D

D

T

E

E

P

Q

Q

M

A

A

A

active site: G98 (≠ E77), H117 (= H96), H119 (= H98), Q138 (≠ Y117), H172 (= H159)
binding zinc ion: H117 (= H96), H119 (= H98), H172 (= H159)

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)
28% identity, 83% coverage: 6:184/216 of query aligns to 3:169/181 of Q58813

query
sites
Q58813

R

K

Q

K

S

Q

L

F

I

I

T

K

A

I

A

C

H

R

R

K

M

L

A

Y

A

D

E

R

G

K

L

Y

N

V

R

V

G

G

T

S

A

G

G

G

N
|
N

L

V

S

S

L

V

R

K

A

E

K

G

L

-

D

-

G

-

V

-

D

D

G

K

F

I

Y

Y

V

L

T

T

P

P

T

T

G

G

M

S

N

I

Y

L

D

G

S

F

L

L

Q

K

A

E

E

D

D

D

I

I

P

A

F

E

V

M

K

D

L

L

A

-

D

D

G

G

S

N

H

V

V

I

G

K

R

G

R

K

L

-

P

P

S

T

S

S

E

E

W

K

R

N

F

L

H

H

R

L

D

M

I

I

Y

Y

A

R

A

K

R

R

P

N

E

D

T

I

G

N

A

A

V

I

L

I

H

H

A

T

H

H

S

S

P

L

F

I

A

S

T

T

S

F

L

L

A

S

C

T

L

I

R

N

R

K

D

E

I

I

-

E

-

L

-

T

P

P

P

E

F

G

H

K

Y

I

M

F

I

L

A

K

R

K

F

I

G

G

G

-

D

-

T

-

V

-

R

-

C

Y

S

V

D

D

Y

Y

A

Y

T

E

F

A

G

G

T

S

Q

L

A

K

L

L

S

A

D

E

T

E

A

-

L

-

A

T

A

A

L

K

E

R

E

D

R

E

K

D

G

V

C

I

L

I

L

L

A

K

N

N

H

H

G

G

M

V

I

V

V

C

C

L

G

G

K

K

D

D

L

L

G

I

E

D

A

A

L

Y

A

-

L

-

G

-

V

I

E

K

L

V

E

E

S

V

L

L

S

E

E

E

Q

Q

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.

P08203 L-ribulose-5-phosphate 4-epimerase AraD; Phosphoribulose isomerase; EC 5.1.3.4 from Escherichia coli (strain K12) (see 4 papers)
27% identity, 84% coverage: 1:182/216 of query aligns to 1:194/231 of P08203

query
sites
P08203

M

M

P

L

A

E

D

D

P

L

R

K

Q

R

S

Q

L

V

I

L

T

E

A

A

A

N

H

L

R

A

M

L

A

P

A

K

E

H

G

N

L

L

N

V

R

T

G

L

T

T

A

W

G

G

N
|
N

L

V

S

S

L

A

R

V

A

D

K

R

L

E

D

R

G

G

V

V

D

-

G

-

F

F

Y

V

V

I

T
x
K

P

P

T

S

G

G

M

V

N

D

Y

Y

D

S

S

V

L

M

Q

T

A

A

E

D

D

D

I

M

P

V

F

V

V

V

K

S

L

I

A

E

D

T

G

G

S

E

H

V

V

V

-

E

G

G

R

T

R

K

L

K

P

P

S

S

E
x
D

W

T

R

P

F

T

H

H

R

R

D

L

I

L

Y

Y

A

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Y
x
T

M

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A

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x
D

F

Y

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F

G

Y

D

G

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T

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D

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Y

K

A

M

T

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-

D

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x
E

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N28 (= N28) mutation to A: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
K42 (≠ T44) mutation to M: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
D76 (≠ E77) 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 (= H96) binding ; mutation to N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+).
H97 (= H98) 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 (≠ Y117) 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 (≠ R121) mutation to N: Loss of the epimerase activity.
E142 (≠ L140) 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 (= H159) binding

Sites not aligning to the query:

218 H→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.
229 Y→F: Loss of the epimerase activity.

1jdiA Crystal structure of l-ribulose-5-phosphate 4-epimerase (see paper)
27% identity, 84% coverage: 1:182/216 of query aligns to 1:194/223 of 1jdiA

query
sites
1jdiA

M

M

P

L

A

E

D

D

P

L

R

K

Q

R

S

Q

L

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I

L

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A

A

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N

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A

D

K

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D

R

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-

G

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F

F

Y

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D

Y

Y

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active site: D76 (≠ E77), H95 (= H96), H97 (= H98), T116 (≠ Y117), D120 (≠ R121), H171 (= H159)
binding zinc ion: H95 (= H96), H97 (= H98), H171 (= H159)

Q988D0 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase; HMPDdc; EC 4.1.1.51 from Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) (Mesorhizobium loti (strain MAFF 303099)) (see paper)
23% identity, 92% coverage: 7:205/216 of query aligns to 7:209/234 of Q988D0

query
sites
Q988D0

Q

E

S

E

L

L

I

V

T

T

A

A

A

T

H

K

R

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A

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H

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G

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K

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A

E73 (= E77) binding
H92 (= H96) binding
H94 (= H98) binding
H163 (= H159) binding

2z7bA Crystal structure of mesorhizobium loti 3-hydroxy-2-methylpyridine-4, 5-dicarboxylate decarboxylase (see paper)
23% identity, 92% coverage: 7:205/216 of query aligns to 10:212/237 of 2z7bA

query
sites
2z7bA

Q

E

S

E

L

L

I

V

T

T

A

A

A

T

H

K

R

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M

L

A

L

A

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G

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M

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D

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M

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A

A

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F

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G

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F

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G

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C

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A

D

D

Y

I

A

A

-

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T

S

F

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G

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Q

A

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A

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M

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H

G

G

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V

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N

C

V

G

G

K

K

D

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L

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R

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L

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A

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E

Y

L

L

E

E

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L

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S

A

E

A

Q

A

F

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T

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A

A

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L

I

G

G

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N

A

V

V

K

L

Y

L

L

D

S

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E

G

Q

E

M

I

A

K

E

T

A

A

binding manganese (ii) ion: E76 (= E77), H95 (= H96), H97 (= H98), H166 (= H159)

Query Sequence

>Dsui_3380 FitnessBrowser__PS:Dsui_3380
MPADPRQSLITAAHRMAAEGLNRGTAGNLSLRAKLDGVDGFYVTPTGMNYDSLQAEDIPF
VKLADGSHVGRRLPSSEWRFHRDIYAARPETGAVLHAHSPFATSLACLRRDIPPFHYMIA
RFGGDTVRCSDYATFGTQALSDTALAALEERKGCLLANHGMIVCGKDLGEALALGVELES
LSEQFWRASQLGSAVLLDTEQMAEALARFATYGKQA

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