SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing 200401 FitnessBrowser__MR1:200401 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 20 (the maximum) hits to proteins with known functional sites (download)

O53289 Phosphoserine phosphatase SerB2; PSP; PSPase; O-phosphoserine phosphohydrolase; Protein-serine/threonine phosphatase; EC 3.1.3.3; EC 3.1.3.16 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
48% identity, 58% coverage: 125:316/330 of query aligns to 181:372/409 of O53289

query
sites
O53289

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D185 (= D129) mutation to G: Completely abolishes enzymatic activity.; mutation to N: Completely abolishes enzymatic activity.
V186 (≠ M130) mutation to Q: Decreases enzymatic activity by 50%.
D187 (= D131) mutation to N: Decreases enzymatic activity by 15%.
S188 (= S132) mutation to A: No effect on enzymatic activity.
S273 (= S217) mutation to A: Completely abolishes enzymatic activity (PubMed:25521849). Decreases enzymatic activity by 60% (PubMed:25037224).
K318 (= K262) mutation to A: Decreases enzymatic activity by 50%.; mutation to E: Completely abolishes enzymatic activity.
D341 (= D285) mutation to G: Decreases enzymatic activity by 80%.; mutation to N: Decreases enzymatic activity by 85%. Completely abolishes enzymatic activity, does not elicit cytoskeletal rearrangements, and does not suppress IL-8 production after TNF-alpha stimulation; when associated with N-345.
D345 (= D289) mutation to N: Decreases enzymatic activity by 55%. Completely abolishes enzymatic activity, does not elicit cytoskeletal rearrangements, and does not suppress IL-8 production after TNF-alpha stimulation; when associated with N-341.

Sites not aligning to the query:

18 G→A: Does not bind L-serine and correspondingly no oligomeric transitions is observed in the presence of L-serine.
108 G→A: Does not bind L-serine and correspondingly no oligomeric transitions is observed in the presence of L-serine.

1f5sA Crystal structure of phosphoserine phosphatase from methanococcus jannaschii (see paper)
42% identity, 63% coverage: 121:327/330 of query aligns to 2:209/210 of 1f5sA

query
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1f5sA

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active site: D10 (= D129), F11 (≠ M130), D12 (= D131), G99 (= G218), K143 (= K262), D170 (= D289)
binding magnesium ion: D10 (= D129), D12 (= D131), D166 (= D285)
binding phosphate ion: D10 (= D129), F11 (≠ M130), D12 (= D131), S98 (= S217), G99 (= G218), K143 (= K262)

1l7nA Transition state analogue of phosphoserine phosphatase (aluminum fluoride complex) (see paper)
42% identity, 63% coverage: 121:327/330 of query aligns to 1:208/209 of 1l7nA

query
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1l7nA

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active site: D9 (= D129), F10 (≠ M130), D11 (= D131), G98 (= G218), K142 (= K262), D169 (= D289)
binding aluminum fluoride: D9 (= D129), F10 (≠ M130), D11 (= D131), S97 (= S217), K142 (= K262)
binding tetrafluoroaluminate ion: D9 (= D129), F10 (≠ M130), D11 (= D131), S97 (= S217), G98 (= G218), K142 (= K262), N168 (= N288)
binding magnesium ion: D9 (= D129), D11 (= D131), D165 (= D285)

Q58989 Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) (see 3 papers)
42% identity, 63% coverage: 121:327/330 of query aligns to 3:210/211 of Q58989

query
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Q58989

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D11 (= D129) active site, Nucleophile; binding ; mutation to N: Loss of activity.
D13 (= D131) active site, Proton donor; binding
E20 (= E138) binding
R56 (= R174) binding
SG 99:100 (= SG 217:218) binding
K144 (= K262) binding
D167 (= D285) binding
N170 (= N288) binding

1l7pA Substrate bound phosphoserine phosphatase complex structure (see paper)
42% identity, 62% coverage: 122:327/330 of query aligns to 1:207/208 of 1l7pA

query
sites
1l7pA

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active site: N8 (≠ D129), F9 (≠ M130), D10 (= D131), G97 (= G218), K141 (= K262), D168 (= D289)
binding phosphoserine: N8 (≠ D129), F9 (≠ M130), D10 (= D131), E17 (= E138), M40 (= M161), F46 (= F167), R53 (= R174), S96 (= S217), G97 (= G218), K141 (= K262)

A0QJI1 Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Mycobacterium avium (strain 104) (see paper)
49% identity, 58% coverage: 125:316/330 of query aligns to 183:374/411 of A0QJI1

query
sites
A0QJI1

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A

R

E

T

L

L

K

R

S

R

H

L

H

G

W

Y

R

A

L

C

V

G

V

V

A

V

S

S

G

G

F

F

T

R

P

R

F

I

V

I

G

E

H

P

L

L

K

A

Q

E

L

E

L

L

N

M

L

L

D

D

A

Y

A

V

F

A

A

A

N

N

E

E

L

L

V

E

I

I

T

V

D

D

G

G

K

T

L

L

A

T

G

G

T

R

V

V

T

V

G

G

K

P

I

I

V

I

D

D

A

R

Q

A

F

G

K

K

A

A

D

T

V

A

V

L

S

R

R

E

C

F

S

A

Q

Q

E

R

W

A

Q

G

I

V

P

P

A

M

G

A

Q

Q

R

T

V

V

A

A

I

V

G

G

D
|
D

G

G

A

A

N

N

D

D

I

I

P

D

M

M

V

L

Q

A

A

A

D

G

F

L

G

G

I

I

A

A

F

F

H

N

A

A

K

K

P

P

K

A

L

L

A

R

A

E

A

V

A

A

D

D

A

A

R

S

I

L

D187 (= D129) binding
D189 (= D131) binding
D343 (= D285) binding

8a21A Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with phenylimidazole (see paper)
49% identity, 58% coverage: 125:316/330 of query aligns to 179:370/396 of 8a21A

query
sites
8a21A

L

L

L

I

V

V

M

F

D
|
D

M

V

D
|
D

S

S

T

T

A

L

I

V

Q

Q

I

G

E
|
E

C
x
V

I
|
I

D

E

E

M

L

L

A

A

M

K

A

A

G

G

V

A

G

E

E

G

Q

Q

V

V

A

A

I

I

T
|
T

E

D

R

A

A

A

M
|
M

Q

R

G

G

E

E

L

L

D

D

F
|
F

E

A

Q

Q

S

S

L

L

R

Q

Q

Q

R
|
R

V

V

A

A

Q

T

L

L

K

A

G

G

A

L

D

P

A

A

K

T

I

V

I

I

H

D

T

E

L

V

C

A

E

G

S

Q

L

L

P

E

F

L

M

M

P

P

G

G

L

A

E

R

A

T

M

T

L

L

A

R

E

T

L

L

K

R

S

R

H

L

H

G

W

Y

R

A

L

C

V

G

V

V

A

V

S

S

G

G

G
|
G

F

F

T

R

P

R

F

I

V

I

G

E

H

P

L

L

K

A

Q

E

L

E

L

L

N

M

L

L

D

D

A

Y

A

V

F

A

A

A

N

N

E

E

L

L

V

E

I

I

T

V

D

D

G

G

K

T

L

L

A

T

G

G

T

R

V

V

T

V

G

G

K

P

I

I

V

I

D

D

A

R

Q

A

F

G

K

K

A

A

D

T

V

A

V

L

S

R

R

E

C

F

S

A

Q

Q

E

R

W

A

Q

G

I

V

P

P

A

M

G

A

Q

Q

R

T

V

V

A

A

I

V

G

G

D
|
D

G

G

A

A

N

N

D

D

I

I

P

D

M

M

V

L

Q

A

A

A

D

G

F

L

G

G

I

I

A

A

F

F

H

N

A

A

K

K

P

P

K

A

L

L

A

R

A

E

A

V

A

A

D

D

A

A

R

S

I

L

binding magnesium ion: D183 (= D129), D185 (= D131), D339 (= D285)
binding 4-phenyl-1h-imidazole: D185 (= D131), E192 (= E138), V193 (≠ C139), I194 (= I140), T211 (= T157), M215 (= M161), F221 (= F167), R228 (= R174), G273 (= G219)

Sites not aligning to the query:

binding 4-phenyl-1h-imidazole: 13, 18, 37

8a1zA Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with 1-(2,4-dichlorophenyl)-3-hydroxyurea (see paper)
49% identity, 58% coverage: 125:316/330 of query aligns to 179:370/396 of 8a1zA

query
sites
8a1zA

L

L

L

I

V

V

M

F

D
|
D

M

V

D
|
D

S

S

T

T

A

L

I

V

Q

Q

I

G

E
|
E

C

V

I

I

D

E

E

M

L

L

A

A

M

K

A

A

G

G

V

A

G

E

E

G

Q

Q

V

V

A

A

I

I

T

T

E

D

R

A

A

A

M
|
M

Q

R

G

G

E

E

L

L

D

D

F
|
F

E

A

Q

Q

S

S

L
|
L

R

Q

Q

Q

R
|
R

V

V

A

A

Q

T

L

L

K

A

G

G

A

L

D

P

A

A

K

T

I

V

I

I

H

D

T

E

L

V

C

A

E

G

S

Q

L

L

P

E

F

L

M

M

P

P

G

G

L

A

E

R

A

T

M

T

L

L

A

R

E

T

L

L

K

R

S

R

H

L

H

G

W

Y

R

A

L

C

V

G

V

V

A

V

S

S

G
|
G

G

G

F
|
F

T

R

P

R

F

I

V

I

G

E

H

P

L

L

K

A

Q

E

L

E

L

L

N

M

L

L

D

D

A

Y

A

V

F

A

A

A

N

N

E

E

L

L

V

E

I

I

T

V

D

D

G

G

K

T

L

L

A

T

G

G

T

R

V

V

T

V

G

G

K

P

I

I

V

I

D

D

A

R

Q

A

F

G

K

K

A

A

D

T

V

A

V

L

S

R

R

E

C

F

S

A

Q

Q

E

R

W

A

Q

G

I

V

P

P

A

M

G

A

Q

Q

R

T

V

V

A

A

I

V

G

G

D
|
D

G

G

A

A

N

N

D

D

I

I

P

D

M

M

V

L

Q

A

A

A

D

G

F

L

G

G

I

I

A

A

F

F

H

N

A

A

K

K

P

P

K

A

L

L

A

R

A

E

A

V

A

A

D

D

A

A

R

S

I

L

binding 1-(2,4-dichlorophenyl)-3-oxidanyl-urea: D185 (= D131), E192 (= E138), M215 (= M161), F221 (= F167), L225 (= L171), R228 (= R174), G272 (= G218), F274 (= F220), D339 (= D285)
binding magnesium ion: D183 (= D129), D185 (= D131), D339 (= D285)

5jlpA Crystal structure of mycobacterium avium serb2 in complex with serine at act domain
49% identity, 58% coverage: 125:316/330 of query aligns to 179:370/396 of 5jlpA

query
sites
5jlpA

L

L

L

I

V

V

M

F

D
|
D

M
x
V

D
|
D

S

S

T

T

A

L

I

V

Q

Q

I

G

E

E

C

V

I

I

D

E

E

M

L

L

A

A

M

K

A

A

G

G

V

A

G

E

E

G

Q

Q

V

V

A

A

I

I

T

T

E

D

R

A

A

A

M

M

Q

R

G

G

E

E

L

L

D

D

F

F

E

A

Q

Q

S

S

L

L

R

Q

Q

Q

R

R

V

V

A

A

Q

T

L

L

K

A

G

G

A

L

D

P

A

A

K

T

I

V

I

I

H

D

T

E

L

V

C

A

E

G

S

Q

L

L

P

E

F

L

M

M

P

P

G

G

L

A

E

R

A

T

M

T

L

L

A

R

E

T

L

L

K

R

S

R

H

L

H

G

W

Y

R

A

L

C

V

G

V

V

A

V

S

S

G
|
G

G

G

F

F

T

R

P

R

F

I

V

I

G

E

H

P

L

L

K

A

Q

E

L

E

L

L

N

M

L

L

D

D

A

Y

A

V

F

A

A

A

N

N

E

E

L

L

V

E

I

I

T

V

D

D

G

G

K

T

L

L

A

T

G

G

T

R

V

V

T

V

G

G

K

P

I

I

V

I

D

D

A

R

Q

A

F

G

K
|
K

A

A

D

T

V

A

V

L

S

R

R

E

C

F

S

A

Q

Q

E

R

W

A

Q

G

I

V

P

P

A

M

G

A

Q

Q

R

T

V

V

A

A

I

V

G

G

D
|
D

G

G

A

A

N

N

D
|
D

I

I

P

D

M

M

V

L

Q

A

A

A

D

G

F

L

G

G

I

I

A

A

F

F

H

N

A

A

K

K

P

P

K

A

L

L

A

R

A

E

A

V

A

A

D

D

A

A

R

S

I

L

active site: D183 (= D129), V184 (≠ M130), D185 (= D131), G272 (= G218), K316 (= K262), D343 (= D289)
binding magnesium ion: D183 (= D129), D339 (= D285)

Sites not aligning to the query:

binding serine: 13, 14

7qplA Crystal structure of phosphoserine phosphatase (serb) from brucella melitensis in complex with phosphate and magnesium
39% identity, 62% coverage: 125:330/330 of query aligns to 82:288/295 of 7qplA

query
sites
7qplA

L

I

L

L

V

I

M

A

D
|
D

M

M

D
|
D

S

S

T

T

A

M

I

I

Q

G

I

Q

E

E

C

C

I

I

D

D

E

E

L

L

A

A

A

E

M

E

A

A

G

G

V

L

G

R

E

D

Q

H

V

V

A

A

I

I

T

T

E

A

R

R

A

A

M

M

Q

N

G

G

E

E

L

I

D

A

F

F

E

E

Q

P

S

A

L

L

R

R

Q

E

R

R

V

V

A

A

Q

L

L

L

K

K

G

G

A

L

D

P

A

L

K

S

I

V

I

I

H

D

T

K

L

V

C

I

E

S

S

T

-

R

L

I

P

T

F

L

M

T

P

P

G

G

L

G

E

P

A

Q

M

L

L

V

A

R

E

T

L

M

K

R

S

K

H

H

H

G

W

A

R

Y

L

T

V

A

V

L

A

V

S

S

G

G

F

F

T

T

P

S

F

F

V

T

G

R

H

R

L

I

K

A

Q

E

L

M

L

I

N

G

L

F

D

N

A

E

F

R

A

A

N

N

E

R

L

L

V

I

I

D

T

D

D

G

G

T

K

R

L

L

A

T

G

G

T

T

V

V

T

A

G

E

K

P

I

I

V

L

D

G

A

R

Q

E

F

A

K

K

A

V

D

E

V

K

V

L

S

V

R

E

C

I

S

A

Q

E

E

R

W

V

Q

G

I

L

P

T

A

P

G

E

Q

D

R

A

V

I

A

A

I

V

G

G

D
|
D

G

G

A

A

N

N

D

D

I

L

P

G

M

M

V

I

Q

Q

A

L

A

A

D

G

F

T

G

G

I

V

A

A

F

L

H

H

A

A

K

K

P

P

K

A

L

V

A

A

A

Q

A

A

D

K

A

M

R

R

I

I

R

D

G

H

L

G

D

D

L

L

R

T

V

A

L

L

P

L

Y

Y

L

I

L

Q

Q

G

F

Y

binding magnesium ion: D86 (= D129), D88 (= D131), D243 (= D285)

1l7oA Crystal structure of phosphoserine phosphatase in apo form (see paper)
40% identity, 62% coverage: 122:327/330 of query aligns to 1:199/200 of 1l7oA

query
sites
1l7oA

K

K

P

K

G

K

L

L

L

I

V

L

M

F

D

N

M

F

D

D

S

S

T

T

A

L

I

V

Q

N

I

N

E

E

C

T

I

I

D

D

E

E

L

I

A

A

A

R

M

E

A

A

G

G

V

V

G

E

E

E

Q

E

V

V

A

K

I

I

T

T

E

-

R

-

A

-

M

-

Q

-

G

-

E

-

L

-

D

N

F

F

E

E

Q

Q

S

S

L

L

R

R

Q

K

R

R

V

V

A

S

Q

L

L

L

K

K

G

D

A

L

D

P

A

I

K

E

I

K

I

V

H

E

T

K

L

A

C

I

E

K

S

R

L

I

P

T

F

P

M

T

P

E

G

G

L

A

E

E

A

E

M

T

L

I

A

K

E

E

L

L

K

K

S

N

H

R

H

G

W

Y

R

V

L

V

V

A

V

V

A

V

S

S

G

G

F

F

T

D

P

I

F

A

V

V

G

N

H

K

L

I

K

K

Q

E

L

K

L

L

N

G

L

L

D

D

A

Y

A

A

F

F

A

A

N

N

E

R

L

L

V

I

I

V

T

K

D

D

G

G

K

K

L

L

A

T

G

G

T

D

V

V

T

E

G

G

K

E

I

V

V

L

D

K

A

E

Q

N

F

A

K

K

A

G

D

E

V

I

V

L

S

E

R

K

C

I

S

A

Q

K

E

I

W

E

Q

G

I

I

P

N

A

L

G

E

Q

D

R

T

V

V

A

A

I

V

G

G

D

D

G

G

A

A

N

N

D

D

I

I

P

S

M

M

V

F

Q

K

A

K

A

A

D

G

F

L

G

K

I

I

A

A

F

F

H

C

A

A

K

K

P

P

K

I

L

L

A

K

A

E

A

K

A

A

D

D

A

I

R
x
C

I

I

R
x
E

G

K

L

R

D

D

L

L

R

R

-

E

V

I

L

L

P

K

Y

Y

L

I

binding zinc ion: C186 (≠ R315), E188 (≠ R317)

3m1yC Crystal structure of a phosphoserine phosphatase (serb) from helicobacter pylori
37% identity, 62% coverage: 125:329/330 of query aligns to 5:208/208 of 3m1yC

query
sites
3m1yC

L

L

L

A

V

V

M

F

D
|
D

M
x
F

D
|
D

S

S

T

T

A

L

I

V

Q

N

I

A

E

E

C

T

I

I

D

E

E

S

L

L

A

A

A

R

M

A

A

W

G

G

V

V

G

F

E

D

Q

E

V

V

A

K

A

T

I

I

T

T

E

L

R

K

A

A

M

M

Q

N

G

G

E

T

L

-

D

D

F

F

E

H

Q

K

S

S

L

L

R

I

Q

L

R

R

V

V

A

S

Q

K

L

L

K

K

G

N

A

M

D

P

A

L

K

K

I

L

I

A

H

K

T

E

L

V

C

C

E

E

S

S

L

L

P

P

F

L

M

F

P

E

G

G

L

A

E

L

A

E

M

L

L

V

A

S

E

A

L

L

K

K

S

E

H

K

H

N

W

Y

R

K

L

V

V

V

V

C

A

F

S

S

G
|
G

G

G

F

F

T

D

P

L

F

A

V

T

G

N

H

H

L

Y

K

R

Q

D

L

L

N

H

L

L

D

D

A

A

F

F

A

S

N

N

E

T

L

L

V

I

I

V

T

E

D

N

G

D

K

A

L

L

A

N

G

G

T

L

V

V

T

T

G

G

K

H

I

M

V

M

D

F

A

S

Q

H

F

S

K
|
K

A

G

D

E

V

M

V

L

S

L

R

V

C

L

S

Q

Q

R

E

L

W

L

Q

N

I

I

P

S

A

K

G

T

Q

N

R

T

V

L

A

V

I

V

G

G

D
|
D

G

G

A

A

N

N

D
|
D

I

L

P

S

M

M

V

F

Q

K

A

H

A

A

D

H

F

I

G

K

I

I

A

A

F

F

H

N

A

A

K

K

P

E

K

V

L

L

A

K

A

Q

A

H

A

A

D

T

A

H

R

C

I

I

R

N

G

E

L

P

D

D

L

L

R

A

V

L

L

I

P

K

Y

P

L

L

L

I

Q

E

active site: D9 (= D129), F10 (≠ M130), D11 (= D131), G97 (= G218), K141 (= K262), D168 (= D289)
binding magnesium ion: D9 (= D129), D11 (= D131), D164 (= D285)

6q6jB Human phosphoserine phosphatase with substrate analogue homo-cysteic acid (see paper)
31% identity, 54% coverage: 126:302/330 of query aligns to 13:192/217 of 6q6jB

query
sites
6q6jB

L

V

V

C

M

F

D
|
D

M
x
V

D
|
D

S

S

T

T

A

V

I

I

Q

R

I

E

E

E

C

G

I

I

D

D

E

E

L

L

A

A

A

K

M

I

A

C

G

G

V

V

G

E

E

D

Q

A

V

V

A

S

A

E

I

M

T

T

E

R

R

R

A

A

M

M

Q

G

G

G

E

A

L

V

D

P

F
|
F

E

K

Q

A

S

A

L

L

R

T

Q

E

R

R

V

L

A

A

Q

L

L

I

K

Q

G

P

A

S

D

R

A

E

K

Q

I

V

I

Q

H

R

T

L

L

I

C

A

E

E

S

Q

L

P

P

P

F

H

M

L

-

T

P

P

G

G

L

I

E

R

A

E

M

L

L

V

A

S

E

R

L

L

K

Q

S

E

H

R

H

N

W

V

R

Q

L

V

V

F

V

L

A

I

S
|
S

G
|
G

F

F

T

R

P

S

F

I

V

V

G

E

H

H

L

V

K

A

Q

S

L

K

L

L

N

N

L

I

D

P

A

A

A

T

-

N

-

V

F

F

A

A

N

N

E

R

L

L

V

K

I

F

T

Y

-

F

D

N

G

G

K

E

L

Y

A

A

G

G

-

F

T

D

V

E

T

T

G

Q

K

P

I

T

V

A

D

E

A

S

Q

G

F

G

K
|
K

A

G

D

K

V

V

V

I

S

K

R

L

C

L

S

K

Q

E

E

K

W

F

Q

H

I

F

P

K

A

-

G

-

Q

K

R

I

V

I

A

M

I

I

G

G

D
|
D

G

G

A

A

N
x
T

D

D

I

M

P

E

M

A

V

C

Q

P

A

P

A

A

D

D

F

A

G

F

I

I

A

G

F

F

binding calcium ion: D16 (= D129), D18 (= D131), D175 (= D285)
binding (2~{S})-2-azanyl-4-sulfo-butanoic acid: D16 (= D129), V17 (≠ M130), D18 (= D131), F54 (= F167), S105 (= S217), G106 (= G218), G107 (= G219), K154 (= K262), T178 (≠ N288)

P78330 Phosphoserine phosphatase; PSP; PSPase; L-3-phosphoserine phosphatase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Homo sapiens (Human) (see 4 papers)
31% identity, 54% coverage: 126:302/330 of query aligns to 17:196/225 of P78330

query
sites
P78330

L

V

V

C

M

F

D
|
D

M
x
V

D
|
D

S
|
S

T

T

A

V

I

I

Q

R

I

E

E
|
E

C

G

I

I

D
|
D

E

E

L

L

A
|
A

A

K

M

I

A

C

G

G

V

V

G

E

E

D

Q

A

V

V

A

S

A

E

I

M

T

T

E

R

R

R

A

A

M
|
M

Q
x
G

G

G

E

A

L

V

D

P

F

F

E

K

Q

A

S

A

L

L

R

T

Q

E

R
|
R

V

L

A

A

Q

L

L

I

K

Q

G

P

A

S

D

R

A

E

K

Q

I

V

I

Q

H

R

T

L

L

I

C

A

E

E

S

Q

L

P

P

P

F

H

M

L

-

T

P

P

G

G

L

I

E

R

A

E

M

L

L

V

A

S

E

R

L

L

K

Q

S

E

H

R

H

N

W

V

R

Q

L

V

V

F

V

L

A

I

S
|
S

G
|
G

F

F

T

R

P

S

F

I

V

V

G

E

H

H

L

V

K

A

Q

S

L

K

L

L

N

N

L

I

D

P

A

A

A

T

-

N

-

V

F

F

A

A

N
|
N

E

R

L

L

V

K

I

F

T

Y

-

F

D

N

G

G

K

E

L

Y

A

A

G

G

-

F

T

D

V

E

T

T

G

Q

K

P

I

T

V

A

D

E

A

S

Q

G

F

G

K
|
K

A

G

D

K

V

V

V

I

S

K

R

L

C

L

S

K

Q

E

E

K

W

F

Q

H

I

F

P

K

A

-

G

-

Q

K

R

I

V

I

A

M

I

I

G

G

D
|
D

G

G

A

A

N
x
T

D

D

I

M

P

E

M

A

V

C

Q

P

A

P

A

A

D

D

F

A

G

F

I

I

A

G

F

F

D20 (= D129) binding
DVD 20:22 (≠ DMD 129:131) binding
D22 (= D131) binding
S23 (= S132) mutation to A: Reduces L-phosphoserine phosphatase activity by about 50%.; mutation to T: Reduces L-phosphoserine phosphatase activity by about 80%.
E29 (= E138) mutation to D: Reduces L-phosphoserine phosphatase activity by about 95%.; mutation to Q: Loss of L-phosphoserine phosphatase activity.
D32 (= D141) to N: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894035
A35 (= A144) to T: in PSPHD; decreased L-phosphoserine phosphatase activity
M52 (= M161) binding ; to T: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894036
G53 (≠ Q162) binding
R65 (= R174) mutation R->A,K: Loss of L-phosphoserine phosphatase activity.
SGG 109:111 (= SGG 217:219) binding ; binding
N133 (= N239) mutation to A: Reduces L-phosphoserine phosphatase activity by about 75%.
K158 (= K262) binding ; binding
D179 (= D285) binding
T182 (≠ N288) binding ; binding ; mutation to S: Reduces L-phosphoserine phosphatase activity by about 99%.; mutation to V: Reduces L-phosphoserine phosphatase activity by about 25%.

Sites not aligning to the query:

202 R→A: Reduces L-phosphoserine phosphatase activity by about 99%.; R→K: Reduces L-phosphoserine phosphatase activity by about 95%.

6hyjB Psph human phosphoserine phosphatase (see paper)
31% identity, 54% coverage: 126:302/330 of query aligns to 17:196/223 of 6hyjB

query
sites
6hyjB

L

V

V

C

M

F

D
|
D

M

V

D
|
D

S

S

T

T

A

V

I

I

Q

R

I

E

E
|
E

C

G

I

I

D

D

E

E

L

L

A

A

A

K

M

I

A

C

G

G

V

V

G

E

E

D

Q

A

V

V

A

S

A

E

I

M

T

T

E

R

R

R

A

A

M

M

Q

G

G

G

E

A

L

V

D

P

F

F

E

K

Q

A

S

A

L

L

R

T

Q

E

R

R

V

L

A

A

Q

L

L

I

K

Q

G

P

A

S

D

R

A

E

K

Q

I

V

I

Q

H

R

T

L

L

I

C

A

E

E

S

Q

L

P

P

P

F

H

M

L

-

T

P

P

G

G

L

I

E

R

A

E

M

L

L

V

A

S

E

R

L

L

K

Q

S

E

H

R

H

N

W

V

R

Q

L

V

V

F

V

L

A

I

S

S

G

G

F

F

T

R

P

S

F

I

V

V

G

E

H

H

L

V

K

A

Q

S

L

K

L

L

N

N

L

I

D

P

A

A

A

T

-

N

-

V

F
|
F

A

A

N

N

E

R

L

L

V

K

I

F

T

Y

-

F

D

N

G

G

K

E

L

Y

A

A

G

G

-

F

T

D

V

E

T

T

G

Q

K

P

I

T

V

A

D

E

A

S

Q

G

F

G

K

K

A

G

D

K

V

V

V

I

S

K

R

L

C

L

S

K

Q

E

E
x
K

W

F

Q

H

I

F

P

K

A

-

G

-

Q

K

R

I

V

I

A

M

I

I

G

G

D
|
D

G

G

A

A

N

T

D

D

I

M

P

E

M

A

V

C

Q

P

A

P

A

A

D

D

F

A

G

F

I

I

A

G

F

F

binding calcium ion: D20 (= D129), D22 (= D131), D179 (= D285)
binding phosphoserine: F131 (= F237), K168 (≠ E272)
binding serine: E29 (= E138)

Sites not aligning to the query:

binding serine: 202

6hyyA Human phosphoserine phosphatase with serine and phosphate (see paper)
31% identity, 54% coverage: 126:302/330 of query aligns to 13:192/221 of 6hyyA

query
sites
6hyyA

L

V

V

C

M

F

D
|
D

M
x
V

D
|
D

S

S

T

T

A

V

I

I

Q

R

I

E

E

E

C

G

I

I

D

D

E

E

L

L

A

A

A

K

M

I

A

C

G

G

V

V

G

E

E

D

Q

A

V

V

A

S

A

E

I

M

T

T

E

R

R

R

A

A

M

M

Q

G

G

G

E

A

L

V

D

P

F

F

E

K

Q

A

S

A

L

L

R

T

Q

E

R

R

V

L

A

A

Q

L

L

I

K

Q

G

P

A

S

D

R

A

E

K

Q

I

V

I

Q

H

R

T

L

L

I

C

A

E

E

S

Q

L

P

P

P

F

H

M

L

-

T

P

P

G

G

L

I

E

R

A

E

M

L

L

V

A

S

E

R

L

L

K

Q

S

E

H

R

H

N

W

V

R

Q

L

V

V

F

V

L

A

I

S
|
S

G
|
G

G

G

F

F

T

R

P

S

F

I

V

V

G

E

H

H

L

V

K

A

Q

S

L

K

L

L

N

N

L

I

D

P

A

A

A

T

-

N

-

V

F

F

A

A

N

N

E

R

L

L

V

K

I

F

T

Y

-

F

D

N

G

G

K

E

L

Y

A

A

G

G

-

F

T

D

V

E

T

T

G

Q

K

P

I

T

V

A

D

E

A

S

Q

G

F

G

K
|
K

A

G

D

K

V

V

V

I

S

K

R

L

C

L

S

K

Q

E

E

K

W

F

Q

H

I

F

P

K

A

-

G

-

Q

K

R

I

V

I

A

M

I

I

G

G

D
|
D

G

G

A

A

N

T

D

D

I

M

P

E

M

A

V

C

Q

P

A

P

A

A

D

D

F

A

G

F

I

I

A

G

F

F

binding magnesium ion: D16 (= D129), D18 (= D131), D175 (= D285)
binding serine: D16 (= D129), V17 (≠ M130), D18 (= D131), S105 (= S217), G106 (= G218), K154 (= K262)

1l8oA Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase (see paper)
31% identity, 54% coverage: 126:302/330 of query aligns to 14:193/222 of 1l8oA

query
sites
1l8oA

L

V

V

C

M

F

D
|
D

M
x
V

D
|
D

S

S

T

T

A

V

I

I

Q

R

I

E

E

E

C

G

I

I

D

D

E

E

L

L

A

A

A

K

M

I

A

C

G

G

V

V

G

E

E

D

Q

A

V

V

A

S

A

E

I

M

T

T

E

R

R

R

A

A

M

M

Q

G

G

G

E

A

L

V

D

P

F

F

E

K

Q

A

S

A

L

L

R

T

Q

E

R

R

V

L

A

A

Q

L

L

I

K

Q

G

P

A

S

D

R

A

E

K

Q

I

V

I

Q

H

R

T

L

L

I

C

A

E

E

S

Q

L

P

P

P

F

H

M

L

-

T

P

P

G

G

L

I

E

R

A

E

M

L

L

V

A

S

E

R

L

L

K

Q

S

E

H

R

H

N

W

V

R

Q

L

V

V

F

V

L

A

I

S
|
S

G
|
G

G

G

F

F

T

R

P

S

F

I

V

V

G

E

H

H

L

V

K

A

Q

S

L

K

L

L

N

N

L

I

D

P

A

A

A

T

-

N

-

V

F

F

A

A

N

N

E

R

L

L

V

K

I

F

T

Y

-

F

D

N

G

G

K

E

L

Y

A

A

G

G

-

F

T

D

V

E

T

T

G

Q

K

P

I

T

V

A

D

E

A

S

Q

G

F

G

K
|
K

A

G

D

K

V

V

V

I

S

K

R

F

C

L

S

K

Q

E

E

K

W

F

Q

H

I

F

P

K

A

-

G

-

Q

K

R

I

V

I

A

M

I

I

G

G

D

D

G
|
G

A

A

N
x
T

D
|
D

I

M

P

E

M

A

V

C

Q

P

A

P

A

A

D

D

F

A

G

F

I

I

A

G

F

F

active site: D17 (= D129), V18 (≠ M130), D19 (= D131), G107 (= G218), K155 (= K262), D180 (= D289)
binding phosphate ion: D17 (= D129), D19 (= D131), S106 (= S217), K155 (= K262)
binding serine: G177 (= G286), T179 (≠ N288)

Sites not aligning to the query:

binding serine: 199

1l8lA Molecular basis for the local confomational rearrangement of human phosphoserine phosphatase (see paper)
31% identity, 54% coverage: 126:302/330 of query aligns to 14:193/222 of 1l8lA

query
sites
1l8lA

L

V

V

C

M

F

D
|
D

M
x
V

D
|
D

S

S

T

T

A

V

I

I

Q

R

I

E

E

E

C

G

I

I

D

D

E

E

L

L

A

A

A

K

M

I

A

C

G

G

V

V

G

E

E

D

Q

A

V

V

A

S

A

E

I

M

T

T

E

R

R

R

A

A

M

M

Q

G

G

G

E

A

L

V

D

P

F

F

E

K

Q

A

S

A

L

L

R

T

Q

E

R

R

V

L

A

A

Q

L

L

I

K

Q

G

P

A

S

D

R

A

E

K

Q

I

V

I

Q

H

R

T

L

L

I

C

A

E

E

S

Q

L

P

P

P

F

H

M

L

-

T

P

P

G

G

L

I

E

R

A

E

M

L

L

V

A

S

E

R

L

L

K

Q

S

E

H

R

H

N

W

V

R

Q

L

V

V

F

V

L

A

I

S

S

G
|
G

G

G

F

F

T

R

P

S

F

I

V

V

G

E

H

H

L

V

K

A

Q

S

L

K

L

L

N

N

L

I

D

P

A

A

A

T

-

N

-

V

F

F

A

A

N

N

E

R

L

L

V

K

I

F

T

Y

-

F

D

N

G

G

K

E

L

Y

A

A

G

G

-

F

T

D

V

E

T

T

G

Q

K

P

I

T

V

A

D

E

A

S

Q

G

F

G

K
|
K

A

G

D

K

V

V

V

I

S

K

R

F

C

L

S

K

Q

E

E

K

W

F

Q

H

I

F

P

K

A

-

G

-

Q

K

R

I

V

I

A

M

I

I

G

G

D
|
D

G
|
G

A

A

N
x
T

D
|
D

I

M

P

E

M

A

V

C

Q

P

A

P

A

A

D

D

F

A

G

F

I

I

A

G

F

F

active site: D17 (= D129), V18 (≠ M130), D19 (= D131), G107 (= G218), K155 (= K262), D180 (= D289)
binding d-2-amino-3-phosphono-propionic acid: D17 (= D129), D19 (= D131), G107 (= G218), K155 (= K262), D176 (= D285), G177 (= G286), T179 (≠ N288)

4ap9A Crystal structure of phosphoserine phosphatase from t.Onnurineus in complex with ndsb-201 (see paper)
28% identity, 56% coverage: 118:301/330 of query aligns to 5:174/200 of 4ap9A

query
sites
4ap9A

P

P

Q

Q

L

F

S

M

K

K

P

K

G

-

L

V

L

A

V

V

M

I

D
|
D

M
x
I

D
x
E

S

G

T

T

A

L

I

T

Q

D

I

F

E

E

C

F

I

W

D

R

E

E

L

M

A

A

A
x
R

M
x
I

A
x
T

G

G

V

K

G

R

E

E

Q

-

V

I

A

E

I

L

T

L

E

E

R

K

A

G

M
x
L

Q

S

G

G

E

E

L

V

D

E

F
x
W

E

L

Q

D

S

S

L

L

R

L

Q

K

R

R

V

V

A

G

Q

L

L

I

K

R

G

G

A

I

D

D

A

E

K

G

I

T

I

F

H

L

T

R

L

T

C

R

E

E

S

K

L

V

P

N

F

V

M

S

P

P

G

E

L

A

E

R

A

E

M

L

L

V

A

E

E

T

L

L

K

R

S

E

H

K

H

G

W

F

R

K

L

V

V

V

V

L

A

I

S

S

G
|
G

G

S

F

F

T

E

P

E

F

V

V

L

G

E

H

P

L

F

K

K

Q

E

L

L

L

-

N

-

L

G

D

D

A

E

A

F

F

M

A

A

N

N

E

R

L

A

V

I

I

F

T

E

D

D

G

G

K

K

L

F

A

Q

G

G

T

-

V

I

T

R

G

L

K

R

I

F

V

R

D
|
D

A

-

Q

-

F

-

K
|
K

A

G

D

E

V

F

V

L

S

K

R

R

C

F

S

R

Q

D

E

-

W

-

Q

-

I

-

P

-

A

-

G

G

Q

F

R

I

V

L

A

A

I

M

G

G

D

D

G

G

A
x
Y

N
x
A

D
|
D

I

A

P

K

M

M

V

F

Q

E

A

R

A

A

D

D

F

M

G

G

I

I

A

A

active site: D15 (= D129), I16 (≠ M130), E17 (≠ D131), G103 (= G218), K141 (= K262), D162 (= D289)
binding 3-pyridinium-1-ylpropane-1-sulfonate: R31 (≠ A145), I32 (≠ M146), T33 (≠ A147), L46 (≠ M161), W52 (≠ F167), D140 (= D258), K141 (= K262), Y160 (≠ A287), A161 (≠ N288)

6iuyA Structure of dsgpdh of dunaliella salina (see paper)
25% identity, 59% coverage: 126:320/330 of query aligns to 17:217/585 of 6iuyA

query
sites
6iuyA

L

V

V

C

M

F

D
|
D

M

V

D
|
D

S

R

T

T

A

V

I

T

Q

T

I

D

E

A

C

S

I

V

D

G

E

L

L

L

A

A

A

K

M

F

A

M

G

G

V

I

G

E

E

D

Q

E

V

A

A

Q

A

S

I

L

T

T

E

E

R

Q

A

A

M

N

Q

R

G

G

E

E

L

I

D

N

F

L

E

T

Q

K

S

A

L

F

R

E

Q

D

R

R

V

L

A

A

Q

K

L

L

K

N

G

F

A

T

D

P

A

T

K

D

I

I

I

D

H

R

T

F

L

L

C

E

E

E

-

H

-

P

-

A

S

H

L

T

P

R

F

L

M

V

P

P

G

G

L

V

E

E

A

N

M

L

L

I

A

A

E

A

L

L

K

K

S

A

H

R

H

G

W

V

R

E

L

V

V

F

V

L

A

I

S

S

G

G

F

F

T

R

-

E

-

M

-

A

-

L

P

P

F

I

V

A

G

S

H

H

L

L

K

K

Q

-

L

-

L

I

N

P

L

A

D

K

A

N

A

V

F

F

A

C

N

N

E

-

L

-

V

-

I

-

T

-

D

-

G

-

K

-

L

-

A

-

G

-

T

T

V

M

T

S

G

W

K

Q

I

L

V

D

D

D

-

H

-

G

-

E

-

P

-

V

-

R

-

L

A

S

Q

H

F

F

K

K

A

S

D

R

V

A

V

I

S

E

R

R

C

I

S

R

Q

R

E

K

W

Y

Q

-

I

-

P

P

A

Y

G

N

Q

N

R

I

V

I

A

M

I

V

G

G

D
|
D

G

G

A

F

N

S

D

D

I

L

P

E

M

A

V

M

Q

Q

-

G

-

S

-

P

-

D

A

G

A

A

D

D

F

A

G

F

I

I

A

C

F

F

H

G

A

G

-

V

-

M

-

Q

K

R

P

P

K

A

L

V

A

A

A

S

A

Q

A

A

D

D

A

W

R

F

I

V

R

R

G

S

L

Y

D

D

binding magnesium ion: D20 (= D129), D22 (= D131), D175 (= D285)

Sites not aligning to the query:

binding nicotinamide-adenine-dinucleotide: 233, 234, 235, 236, 268, 290, 321, 324, 349, 381, 382, 497, 529, 530, 532

Query Sequence

>200401 FitnessBrowser__MR1:200401
MESLNQNPLFVWLAASPSPRFEYQGICFEAYQESSMRPSLSQFAMRLIYEDISLEDALAT
WIVSLAKSLKLTSLSIAPIRRQVALHCVELALPVEPTAELLATFPLQAELHLIRGPLPQL
SKPGLLVMDMDSTAIQIECIDELAAMAGVGEQVAAITERAMQGELDFEQSLRQRVAQLKG
ADAKIIHTLCESLPFMPGLEAMLAELKSHHWRLVVASGGFTPFVGHLKQLLNLDAAFANE
LVITDGKLAGTVTGKIVDAQFKADVVSRCSQEWQIPAGQRVAIGDGANDIPMVQAADFGI
AFHAKPKLAAAADARIRGLDLRVLPYLLQF

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