SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_092058844.1 NCBI__GCF_900111775.1:WP_092058844.1 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)
40% identity, 97% coverage: 6:393/398 of query aligns to 7:391/409 of O53289

query
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O53289

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G18 (= G17) mutation to A: Does not bind L-serine and correspondingly no oligomeric transitions is observed in the presence of L-serine.
G108 (≠ L109) mutation to A: Does not bind L-serine and correspondingly no oligomeric transitions is observed in the presence of L-serine.
D185 (= D187) mutation to G: Completely abolishes enzymatic activity.; mutation to N: Completely abolishes enzymatic activity.
V186 (≠ M188) mutation to Q: Decreases enzymatic activity by 50%.
D187 (= D189) mutation to N: Decreases enzymatic activity by 15%.
S188 (= S190) mutation to A: No effect on enzymatic activity.
S273 (= S275) mutation to A: Completely abolishes enzymatic activity (PubMed:25521849). Decreases enzymatic activity by 60% (PubMed:25037224).
K318 (= K320) mutation to A: Decreases enzymatic activity by 50%.; mutation to E: Completely abolishes enzymatic activity.
D341 (= D343) 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 (= D347) 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.

8a21A Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with phenylimidazole (see paper)
40% identity, 97% coverage: 6:393/398 of query aligns to 5:389/396 of 8a21A

query
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8a21A

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binding magnesium ion: D183 (= D187), D185 (= D189), D339 (= D343)
binding 4-phenyl-1h-imidazole: D13 (= D14), T18 (≠ I19), Q37 (= Q38), D185 (= D189), E192 (= E196), V193 (= V197), I194 (= I198), T211 (= T215), M215 (= M219), F221 (= F225), R228 (= R232), G273 (= G277)

8a1zA Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with 1-(2,4-dichlorophenyl)-3-hydroxyurea (see paper)
40% identity, 97% coverage: 6:393/398 of query aligns to 5:389/396 of 8a1zA

query
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8a1zA

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binding 1-(2,4-dichlorophenyl)-3-oxidanyl-urea: D185 (= D189), E192 (= E196), M215 (= M219), F221 (= F225), L225 (= L229), R228 (= R232), G272 (= G276), F274 (= F278), D339 (= D343)
binding magnesium ion: D183 (= D187), D185 (= D189), D339 (= D343)

5jlpA Crystal structure of mycobacterium avium serb2 in complex with serine at act domain
40% identity, 97% coverage: 6:393/398 of query aligns to 5:389/396 of 5jlpA

query
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5jlpA

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A

A

A

T

V

L

T

F

G

E

H

V

I

L

A

S

E

R

A

H

G

G

A

V

R

E

I

L

R

L

D

N

I

V

E

E

Q

Q

S

V

V

V

T

I

H

R

T

H

L

R

L

L

S

T

L

L

S

G

V

V

L

L

I

V

D

C

F

C

P

P

T

A

G

D

E

V

S

A

D

D

Q

G

K

P

P

A

L

L

V

R

K

H

E

D

L

V

L

E

F

A

L

A

A

I

K

R

E

K

L

V

G

G

L

L

D

D

L

V

D

S

F

I

Q

E

V

R

L

S

S

D

E

D

A

V

E

P

Y

I

R

I

R

R

K

E

T

P

T

S

R

-

N

-

A

T

Y

H

V

T

V

I

T

F

I

V

L

L

G

G

G

R

E

P

V

I

N

T

A

A

L

A

A

A

L

F

A

G

R

A

V

V

S

A

R

R

I

E

L

V

A

A

E

A

H

L

A

G

V

V

N

N

I

I

E

D

R

L

I

I

S

R

K

G

L

V

T

S

Q

D

G

Y

Q

P

L

V

R

I

C

G

V

L

E

E

F

L

L

R

I

V

T

S

T

V

T

P

P

P

D

G

L

A

D

D

V

G

K

A

V

L

M

R

T

T

R

-

K

A

L

L

L

N

H

R

T

V

G

S

A

S

S

E

V

E

G

H

V

V

D

D

I

V

A

A

V

V

Q

E

K

D

E

Y

S

T

L

L

Y

E

R

R

A

A

K

K

R

R

L

L

V

I

V

V

M

F

D
|
D

M
x
V

D
|
D

S

S

T

T

L

L

I

V

Q

Q

V

G

E

E

V

V

I

I

D

E

E

M

L

L

A

A

R

A

V

K

A

A

G

G

V

A

G

E

E

G

Q

Q

V

V

A

A

E

A

I

I

T

T

E

D

R

A

A

A

M

M

N

R

G

G

E

E

L

L

D

D

F

F

S

A

G

Q

A

S

L

L

R

Q

E

Q

R

R

V

V

A

A

L

T

L

L

K

A

G

G

L

L

K

P

A

A

E

T

A

V

L

I

E

D

Q

E

V

V

Y

A

R

G

N

Q

I

L

P

E

L

L

T

M

P

P

G

G

A

A

R

R

N

T

L

T

V

L

T

R

I

T

L

L

K

R

R

R

L

L

G

G

F

Y

K

A

T

C

A

G

V

V

I

V

S

S

G
|
G

G

G

F

F

Q

R

F

R

F

I

T

I

D

E

R

P

L

L

K

A

S

E

D

E

L

L

G

M

L

L

D

D

Y

Y

A

V

Y

A

A

A

N

N

G

E

L

L

E

E

I

I

V

V

D

D

G

G

I

T

V

L

T

T

G

G

E

R

V

V

A

V

G

G

T

P

I

I

V

I

D

D

G

R

A

A

R

G

K
|
K

A

A

Q

T

L

A

L

L

E

R

E

E

I

F

A

A

G

Q

K

R

E

A

G

G

I

V

T

P

L

M

D

A

Q

Q

A

T

I

V

A

A

I

V

G

G

D
|
D

G

G

A

A

N

N

D
|
D

L

I

P

D

M

M

L

L

G

A

R

A

A

A

G

G

L

L

G

G

I

I

A

A

F

F

N

N

A

A

K

K

A

P

R

A

V

L

R

R

E

E

Q

V

A

A

D

D

F

A

H

S

I

L

N

S

Q

H

Q

P

N

Y

L

L

D

D

S

T

I

V

L

L

Y

F

L

L

I

L

G

G

L

V

S

T

E

R

R

G

E

E

M

I

active site: D183 (= D187), V184 (≠ M188), D185 (= D189), G272 (= G276), K316 (= K320), D343 (= D347)
binding magnesium ion: D183 (= D187), D339 (= D343)
binding serine: D13 (= D14), Q14 (≠ R15)

A0QJI1 Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Mycobacterium avium (strain 104) (see paper)
40% identity, 97% coverage: 6:393/398 of query aligns to 9:393/411 of A0QJI1

query
sites
A0QJI1

V

V

L

L

L

I

T

T

L

V

T

T

G

G

P

V

D

D

R

Q

T

P

G

G

I

V

I

T

A

A

A

T

V

L

T

F

G

E

H

V

I

L

A

S

E

G

A

H

G

G

A

V

R

E

I

L

R

L

D

N

I

V

E

E

Q

Q

S

V

V

V

T

I

H

R

T

H

L

R

L

L

S

T

L

L

S

G

V

V

L

L

I

V

D

C

F

C

P

P

T

A

G

D

E

V

S

A

D

D

Q

G

K

P

P

A

L

L

V

R

K

H

E

D

L

V

L

E

F

A

L

A

A

I

K

R

E

K

L

V

G

G

L

L

D

D

L

V

D

S

F

I

Q

E

V

R

L

S

S

D

E

D

A

V

E

P

Y

I

R

I

R

R

K

E

T

P

T

S

R

-

N

-

A

T

Y

H

V

T

V

I

T

F

I

V

L

L

G

G

G

R

E

P

V

I

N

T

A

A

L

A

A

A

L

F

A

G

R

A

V

V

S

A

R

R

I

E

L

V

A

A

E

A

H

L

A

G

V

V

N

N

I

I

E

D

R

L

I

I

S

R

K

G

L

V

T

S

Q

D

G

Y

Q

P

L

V

R

I

C

G

V

L

E

E

F

L

L

R

I

V

T

S

T

V

T

P

P

P

D

G

L

A

D

D

V

G

K

A

V

L

M

R

T

T

R

-

K

A

L

L

L

N

H

R

T

V

G

S

A

S

S

E

V

E

G

H

V

V

D

D

I

V

A

A

V

V

Q

E

K

D

E

Y

S

T

L

L

Y

E

R

R

A

A

K

K

R

R

L

L

V

I

V

V

M

F

D
|
D

M

V

D
|
D

S

S

T

T

L

L

I

V

Q

Q

V

G

E

E

V

V

I

I

D

E

E

M

L

L

A

A

R

A

V

K

A

A

G

G

V

A

G

E

E

G

Q

Q

V

V

A

A

E

A

I

I

T

T

E

D

R

A

A

A

M

M

N

R

G

G

E

E

L

L

D

D

F

F

S

A

G

Q

A

S

L

L

R

Q

E

Q

R

R

V

V

A

A

L

T

L

L

K

A

G

G

L

L

K

P

A

A

E

T

A

V

L

I

E

D

Q

E

V

V

Y

A

R

G

N

Q

I

L

P

E

L

L

T

M

P

P

G

G

A

A

R

R

N

T

L

T

V

L

T

R

I

T

L

L

K

R

R

R

L

L

G

G

F

Y

K

A

T

C

A

G

V

V

I

V

S

S

G

G

F

F

Q

R

F

R

F

I

T

I

D

E

R

P

L

L

K

A

S

E

D

E

L

L

G

M

L

L

D

D

Y

Y

A

V

Y

A

A

A

N

N

G

E

L

L

E

E

I

I

V

V

D

D

G

G

I

T

V

L

T

T

G

G

E

R

V

V

A

V

G

G

T

P

I

I

V

I

D

D

G

R

A

A

R

G

K

K

A

A

Q

T

L

A

L

L

E

R

E

E

I

F

A

A

G

Q

K

R

E

A

G

G

I

V

T

P

L

M

D

A

Q

Q

A

T

I

V

A

A

I

V

G

G

D
|
D

G

G

A

A

N

N

D

D

L

I

P

D

M

M

L

L

G

A

R

A

A

A

G

G

L

L

G

G

I

I

A

A

F

F

N

N

A

A

K

K

A

P

R

A

V

L

R

R

E

E

Q

V

A

A

D

D

F

A

H

S

I

L

N

S

Q

H

Q

P

N

Y

L

L

D

D

S

T

I

V

L

L

Y

F

L

L

I

L

G

G

L

V

S

T

E

R

R

G

E

E

M

I

D187 (= D187) binding Mg(2+)
D189 (= D189) binding Mg(2+)
D343 (= D343) binding Mg(2+)

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)
47% identity, 52% coverage: 179:386/398 of query aligns to 3:210/211 of Q58989

query
sites
Q58989

R

K

A

K

K

K

R

K

L

L

V

I

V

L

M

F

D
|
D

M

F

D
|
D

S

S

T

T

L

L

I

V

Q

N

V

N

E
|
E

V

T

I

I

D

D

E

E

L

I

A

A

R

R

V

E

A

A

G

G

V

V

G

E

E

E

Q

E

V

V

A

K

E

K

I

I

T

T

E

K

R

E

A

A

M

M

N

E

G

G

E

K

L

L

D

N

F

F

S

E

G

Q

A

S

L

L

R

R

E

K

R
|
R

V

V

A

S

L

L

K

K

G

D

L

L

K

P

A

I

E

E

A

K

L

V

E

E

Q

K

V

A

Y

I

R

K

N

R

I

I

P

T

L

P

T

T

P

E

G

G

A

A

R

E

N

E

L

T

V

I

T

K

I

E

L

L

K

K

R

N

L

R

G

G

F

Y

K

V

T

V

A

A

V

V

I

V

S
|
S

G
|
G

G

G

F

F

Q

D

F

I

F

A

T

V

D

N

R

K

L

I

K

K

S

E

D

K

L

L

G

G

L

L

D

D

Y

Y

A

A

Y

F

A

A

N

N

G

R

L

L

E

I

I

V

V

K

D

D

G

G

I

K

V

L

T

T

G

G

E

D

V

V

A

E

G

G

T

E

I

V

V

L

D

K

G

E

A

N

R

A

K
|
K

A

G

Q

E

L

I

L

L

E

E

E

K

I

I

A

A

G

K

K

I

E

E

G

G

I

I

T

N

L

L

D

E

Q

D

A

T

I

V

A

A

I

V

G

G

D
|
D

G

G

A

A

N
|
N

D

D

L

I

P

S

M

M

L

F

G

K

R

K

A

A

G

G

L

L

G

K

I

I

A

A

F

F

N

C

A

A

K

K

A

P

R

I

V

L

R

K

E

E

Q

K

A

A

D

D

F

I

H

C

I

I

N

E

Q

K

Q

R

N

D

L

L

D

R

S

E

I

I

L

L

Y

K

L

Y

I

I

D11 (= D187) active site, Nucleophile; binding Mg(2+); mutation to N: Loss of activity.
D13 (= D189) active site, Proton donor; binding Mg(2+)
E20 (= E196) binding substrate
R56 (= R232) binding substrate
SG 99:100 (= SG 275:276) binding substrate
K144 (= K320) binding substrate
D167 (= D343) binding Mg(2+)
N170 (= N346) binding substrate

1f5sA Crystal structure of phosphoserine phosphatase from methanococcus jannaschii (see paper)
47% identity, 52% coverage: 179:386/398 of query aligns to 2:209/210 of 1f5sA

query
sites
1f5sA

R

K

A

K

K

K

R

K

L

L

V

I

V

L

M

F

D
|
D

M
x
F

D
|
D

S

S

T

T

L

L

I

V

Q

N

V

N

E

E

V

T

I

I

D

D

E

E

L

I

A

A

R

R

V

E

A

A

G

G

V

V

G

E

E

E

Q

E

V

V

A

K

E

K

I

I

T

T

E

K

R

E

A

A

M

M

N

E

G

G

E

K

L

L

D

N

F

F

S

E

G

Q

A

S

L

L

R

R

E

K

R

R

V

V

A

S

L

L

K

K

G

D

L

L

K

P

A

I

E

E

A

K

L

V

E

E

Q

K

V

A

Y

I

R

K

N

R

I

I

P

T

L

P

T

T

P

E

G

G

A

A

R

E

N

E

L

T

V

I

T

K

I

E

L

L

K

K

R

N

L

R

G

G

F

Y

K

V

T

V

A

A

V

V

I

V

S
|
S

G
|
G

G

G

F

F

Q

D

F

I

F

A

T

V

D

N

R

K

L

I

K

K

S

E

D

K

L

L

G

G

L

L

D

D

Y

Y

A

A

Y

F

A

A

N

N

G

R

L

L

E

I

I

V

V

K

D

D

G

G

I

K

V

L

T

T

G

G

E

D

V

V

A

E

G

G

T

E

I

V

V

L

D

K

G

E

A

N

R

A

K
|
K

A

G

Q

E

L

I

L

L

E

E

E

K

I

I

A

A

G

K

K

I

E

E

G

G

I

I

T

N

L

L

D

E

Q

D

A

T

I

V

A

A

I

V

G

G

D
|
D

G

G

A

A

N

N

D
|
D

L

I

P

S

M

M

L

F

G

K

R

K

A

A

G

G

L

L

G

K

I

I

A

A

F

F

N

C

A

A

K

K

A

P

R

I

V

L

R

K

E

E

Q

K

A

A

D

D

F

I

H

C

I

I

N

E

Q

K

Q

R

N

D

L

L

D

R

S

E

I

I

L

L

Y

K

L

Y

I

I

active site: D10 (= D187), F11 (≠ M188), D12 (= D189), G99 (= G276), K143 (= K320), D170 (= D347)
binding magnesium ion: D10 (= D187), D12 (= D189), D166 (= D343)
binding phosphate ion: D10 (= D187), F11 (≠ M188), D12 (= D189), S98 (= S275), G99 (= G276), K143 (= K320)

1l7nA Transition state analogue of phosphoserine phosphatase (aluminum fluoride complex) (see paper)
47% identity, 52% coverage: 179:386/398 of query aligns to 1:208/209 of 1l7nA

query
sites
1l7nA

R

K

A

K

K

K

R

K

L

L

V

I

V

L

M

F

D
|
D

M
x
F

D
|
D

S

S

T

T

L

L

I

V

Q

N

V

N

E

E

V

T

I

I

D

D

E

E

L

I

A

A

R

R

V

E

A

A

G

G

V

V

G

E

E

E

Q

E

V

V

A

K

E

K

I

I

T

T

E

K

R

E

A

A

M

M

N

E

G

G

E

K

L

L

D

N

F

F

S

E

G

Q

A

S

L

L

R

R

E

K

R

R

V

V

A

S

L

L

K

K

G

D

L

L

K

P

A

I

E

E

A

K

L

V

E

E

Q

K

V

A

Y

I

R

K

N

R

I

I

P

T

L

P

T

T

P

E

G

G

A

A

R

E

N

E

L

T

V

I

T

K

I

E

L

L

K

K

R

N

L

R

G

G

F

Y

K

V

T

V

A

A

V

V

I

V

S
|
S

G
|
G

G

G

F

F

Q

D

F

I

F

A

T

V

D

N

R

K

L

I

K

K

S

E

D

K

L

L

G

G

L

L

D

D

Y

Y

A

A

Y

F

A

A

N

N

G

R

L

L

E

I

I

V

V

K

D

D

G

G

I

K

V

L

T

T

G

G

E

D

V

V

A

E

G

G

T

E

I

V

V

L

D

K

G

E

A

N

R

A

K
|
K

A

G

Q

E

L

I

L

L

E

E

E

K

I

I

A

A

G

K

K

I

E

E

G

G

I

I

T

N

L

L

D

E

Q

D

A

T

I

V

A

A

I

V

G

G

D
|
D

G

G

A

A

N
|
N

D
|
D

L

I

P

S

M

M

L

F

G

K

R

K

A

A

G

G

L

L

G

K

I

I

A

A

F

F

N

C

A

A

K

K

A

P

R

I

V

L

R

K

E

E

Q

K

A

A

D

D

F

I

H

C

I

I

N

E

Q

K

Q

R

N

D

L

L

D

R

S

E

I

I

L

L

Y

K

L

Y

I

I

active site: D9 (= D187), F10 (≠ M188), D11 (= D189), G98 (= G276), K142 (= K320), D169 (= D347)
binding aluminum fluoride: D9 (= D187), F10 (≠ M188), D11 (= D189), S97 (= S275), K142 (= K320)
binding tetrafluoroaluminate ion: D9 (= D187), F10 (≠ M188), D11 (= D189), S97 (= S275), G98 (= G276), K142 (= K320), N168 (= N346)
binding magnesium ion: D9 (= D187), D11 (= D189), D165 (= D343)

1l7pA Substrate bound phosphoserine phosphatase complex structure (see paper)
47% identity, 52% coverage: 181:386/398 of query aligns to 2:207/208 of 1l7pA

query
sites
1l7pA

K

K

R

K

L

L

V

I

V

L

M

F

D
x
N

M
x
F

D
|
D

S

S

T

T

L

L

I

V

Q

N

V

N

E
|
E

V

T

I

I

D

D

E

E

L

I

A

A

R

R

V

E

A

A

G

G

V

V

G

E

E

E

Q

E

V

V

A

K

E

K

I

I

T

T

E

K

R

E

A

A

M
|
M

N

E

G

G

E

K

L

L

D

N

F
|
F

S

E

G

Q

A

S

L

L

R

R

E

K

R
|
R

V

V

A

S

L

L

K

K

G

D

L

L

K

P

A

I

E

E

A

K

L

V

E

E

Q

K

V

A

Y

I

R

K

N

R

I

I

P

T

L

P

T

T

P

E

G

G

A

A

R

E

N

E

L

T

V

I

T

K

I

E

L

L

K

K

R

N

L

R

G

G

F

Y

K

V

T

V

A

A

V

V

I

V

S
|
S

G
|
G

G

G

F

F

Q

D

F

I

F

A

T

V

D

N

R

K

L

I

K

K

S

E

D

K

L

L

G

G

L

L

D

D

Y

Y

A

A

Y

F

A

A

N

N

G

R

L

L

E

I

I

V

V

K

D

D

G

G

I

K

V

L

T

T

G

G

E

D

V

V

A

E

G

G

T

E

I

V

V

L

D

K

G

E

A

N

R

A

K
|
K

A

G

Q

E

L

I

L

L

E

E

E

K

I

I

A

A

G

K

K

I

E

E

G

G

I

I

T

N

L

L

D

E

Q

D

A

T

I

V

A

A

I

V

G

G

D

D

G

G

A

A

N

N

D
|
D

L

I

P

S

M

M

L

F

G

K

R

K

A

A

G

G

L

L

G

K

I

I

A

A

F

F

N

C

A

A

K

K

A

P

R

I

V

L

R

K

E

E

Q

K

A

A

D

D

F

I

H

C

I

I

N

E

Q

K

Q

R

N

D

L

L

D

R

S

E

I

I

L

L

Y

K

L

Y

I

I

active site: N8 (≠ D187), F9 (≠ M188), D10 (= D189), G97 (= G276), K141 (= K320), D168 (= D347)
binding phosphoserine: N8 (≠ D187), F9 (≠ M188), D10 (= D189), E17 (= E196), M40 (= M219), F46 (= F225), R53 (= R232), S96 (= S275), G97 (= G276), K141 (= K320)

7qplA Crystal structure of phosphoserine phosphatase (serb) from brucella melitensis in complex with phosphate and magnesium
47% identity, 56% coverage: 167:387/398 of query aligns to 68:287/295 of 7qplA

query
sites
7qplA

V

I

D

D

I

V

A

V

V

V

Q

Q

K

E

E

Q

S

E

L

-

Y

-

R

R

A

R

K

K

R

K

L

I

V

L

V

I

M

A

D
|
D

M

M

D
|
D

S

S

T

T

L

M

I

I

Q

G

V

Q

E

E

V

C

I

I

D

D

E

E

L

L

A

A

R

E

V

E

A

A

G

G

V

L

G

R

E

D

Q

H

V

V

A

A

E

A

I

I

T

T

E

A

R

R

A

A

M

M

N

N

G

G

E

E

L

I

D

A

F

F

S

E

G

P

A

A

L

L

R

R

E

E

R

R

V

V

A

A

L

L

K

K

G

G

L

L

K

P

A

L

E

S

A

V

L

I

E

D

Q

K

V

V

Y

I

R

S

N

T

-

R

I

I

P

T

L

L

T

T

P

P

G

G

A

G

R

P

N

Q

L

L

V

V

T

R

I

T

L

M

K

R

R

K

L

H

G

G

F

A

K

Y

T

T

A

A

V

L

I

V

S

S

G

G

F

F

Q

T

F

S

F

F

T

T

D

R

R

R

L

I

K

A

S

E

D

M

L

I

G

G

L

F

D

N

Y

E

A

E

Y

R

A

A

N

N

G

R

L

L

E

-

I

I

V

D

D

D

G

G

I

T

-

R

V

L

T

T

G

G

E

T

V

V

A

A

G

E

T

P

I

I

V

L

D

G

G

R

A

E

R

A

K

K

A

V

Q

E

L

K

L

L

E

V

E

E

I

I

A

A

G

E

K

R

E

V

G

G

I

L

T

T

L

P

D

E

Q

D

A

A

I

I

A

A

I

V

G

G

D
|
D

G

G

A

A

N

N

D

D

L

L

P

G

M

M

L

I

G

Q

R

L

A

A

G

G

L

T

G

G

I

V

A

A

F

L

N

H

A

A

K

K

A

P

R

A

V

V

R

A

E

A

Q

Q

A

A

D

K

F

M

H

R

I

I

N

D

Q

H

Q

G

N

D

L

L

D

T

S

A

I

L

L

L

Y

Y

L

I

I

Q

G

G

binding magnesium ion: D86 (= D187), D88 (= D189), D243 (= D343)

1l7oA Crystal structure of phosphoserine phosphatase in apo form (see paper)
45% identity, 52% coverage: 181:386/398 of query aligns to 2:199/200 of 1l7oA

query
sites
1l7oA

K

K

R

K

L

L

V

I

V

L

M

F

D

N

M

F

D

D

S

S

T

T

L

L

I

V

Q

N

V

N

E

E

V

T

I

I

D

D

E

E

L

I

A

A

R

R

V

E

A

A

G

G

V

V

G

E

E

E

Q

E

V

V

A

K

E

K

I

I

T

T

E

-

R

-

A

-

M

-

N

-

G

-

E

-

L

-

D

N

F

F

S

E

G

Q

A

S

L

L

R

R

E

K

R

R

V

V

A

S

L

L

K

K

G

D

L

L

K

P

A

I

E

E

A

K

L

V

E

E

Q

K

V

A

Y

I

R

K

N

R

I

I

P

T

L

P

T

T

P

E

G

G

A

A

R

E

N

E

L

T

V

I

T

K

I

E

L

L

K

K

R

N

L

R

G

G

F

Y

K

V

T

V

A

A

V

V

I

V

S

S

G

G

F

F

Q

D

F

I

F

A

T

V

D

N

R

K

L

I

K

K

S

E

D

K

L

L

G

G

L

L

D

D

Y

Y

A

A

Y

F

A

A

N

N

G

R

L

L

E

I

I

V

V

K

D

D

G

G

I

K

V

L

T

T

G

G

E

D

V

V

A

E

G

G

T

E

I

V

V

L

D

K

G

E

A

N

R

A

K

K

A

G

Q

E

L

I

L

L

E

E

E

K

I

I

A

A

G

K

K

I

E

E

G

G

I

I

T

N

L

L

D

E

Q

D

A

T

I

V

A

A

I

V

G

G

D

D

G

G

A

A

N

N

D

D

L

I

P

S

M

M

L

F

G

K

R

K

A

A

G

G

L

L

G

K

I

I

A

A

F

F

N

C

A

A

K

K

A

P

R

I

V

L

R

K

E

E

Q

K

A

A

D

D

F

I

H
x
C

I

I

N
x
E

Q

K

Q

R

N

D

L

L

D

R

S

E

I

I

L

L

Y

K

L

Y

I

I

binding zinc ion: C186 (≠ H373), E188 (≠ N375)

3m1yC Crystal structure of a phosphoserine phosphatase (serb) from helicobacter pylori
37% identity, 52% coverage: 181:386/398 of query aligns to 3:207/208 of 3m1yC

query
sites
3m1yC

K

Q

R

K

L

L

V

A

V

V

M

F

D
|
D

M
x
F

D
|
D

S

S

T

T

L

L

I

V

Q

N

V

A

E

E

V

T

I

I

D

E

E

S

L

L

A

A

R

R

V

A

A

W

G

G

V

V

G

F

E

D

Q

E

V

V

A

K

E

T

I

I

T

T

E

L

R

K

A

A

M

M

N

N

G

G

E

T

L

-

D

D

F

F

S

H

G

K

A

S

L

L

R

I

E

L

R

R

V

V

A

S

L

K

L

L

K

K

G

N

L

M

K

P

A

L

E

K

A

L

L

A

E

K

Q

E

V

V

Y

C

R

E

N

S

I

L

P

P

L

L

T

F

P

E

G

G

A

A

R

L

N

E

L

L

V

V

T

S

I

A

L

L

K

K

R

E

L

K

G

N

F

Y

K

K

T

V

A

V

V

C

I

F

S

S

G
|
G

G

G

F

F

Q

D

F

L

F

A

T

T

D

N

R

H

L

Y

K

R

S

D

D

L

L

L

G

H

L

L

D

D

Y

A

A

A

Y

F

A

S

N

N

G

T

L

L

E

I

I

V

V

E

D

N

G

D

I

A

V

L

T

N

G

G

E

L

V

V

A

T

G

G

T

H

I

M

V

M

D

F

G

S

A

H

R

S

K
|
K

A

G

Q

E

L

M

L

L

E

L

E

V

I

L

A

Q

G

R

K

L

E

L

G

N

I

I

T

S

L

K

D

T

Q

N

A

T

I

L

A

V

I

V

G

G

D
|
D

G

G

A

A

N

N

D
|
D

L

L

P

S

M

M

L

F

G

K

R

H

A

A

G

H

L

I

G

K

I

I

A

A

F

F

N

N

A

A

K

K

A

E

R

V

V

L

R

K

E

Q

Q

H

A

A

D

T

F

H

H

C

I

I

N

N

Q

E

Q

P

N

D

L

L

D

A

S

L

I

I

L

K

Y

P

L

L

I

I

active site: D9 (= D187), F10 (≠ M188), D11 (= D189), G97 (= G276), K141 (= K320), D168 (= D347)
binding magnesium ion: D9 (= D187), D11 (= D189), D164 (= D343)

1l8oA Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase (see paper)
33% identity, 48% coverage: 184:374/398 of query aligns to 14:210/222 of 1l8oA

query
sites
1l8oA

V

V

V

C

M

F

D
|
D

M
x
V

D
|
D

S

S

T

T

L

V

I

I

Q

R

V

E

E

E

V

G

I

I

D

D

E

E

L

L

A

A

R

K

V

I

A

C

G

G

V

V

G

E

E

D

Q

A

V

V

A

S

E

E

I

M

T

T

E

R

R

R

A

A

M

M

N

G

G

G

E

A

L

V

D

P

F

F

S

K

G

A

A

A

L

L

R

T

E

E

R

R

V

L

A

A

L

L

L

I

K

Q

G

P

L

S

K

R

A

E

E

Q

A

V

L

Q

E

R

Q

L

V

I

Y

A

R

E

N

Q

I

P

P

P

-

H

L

L

T

T

P

P

G

G

A

I

R

R

N

E

L

L

V

V

T

S

I

R

L

L

K

Q

R

E

L

R

G

N

F

V

K

Q

T

V

A

F

V

L

I

I

S
|
S

G
|
G

G

G

F

F

Q

R

F

S

F

I

T

V

D

E

R

H

L

V

K

A

S

S

D

K

L

L

G

N

L

I

D

P

Y

A

A

T

-

N

-

V

Y

F

A

A

N

N

G

R

L

L

E

K

I

F

V

Y

D

-

G

-

I

-

V

F

T

N

G

G

E

E

V

Y

A

A

G

G

-

F

-

D

-

E

-

T

-

Q

T

P

I

T

V

A

D

E

G

S

A

G

R

G

K
|
K

A

G

Q

K

L

V

L

I

E

K

E

F

I

L

A

-

G

-

K

K

E

E

G

K

I

F

T

H

L

F

D

K

Q

K

A

I

I

I

A

M

I

I

G

G

D

D

G
|
G

A

A

N
x
T

D
|
D

L

M

P

E

M

A

L

C

G

P

R

P

A

A

G

D

L

A

G

F

I

I

A

G

F

F

N

G

A

G

-

N

-

V

-

I

K
x
R

A

Q

R

Q

V

V

R

K

E

D

Q

N

A

A

D

K

F

W

H

Y

I

I

active site: D17 (= D187), V18 (≠ M188), D19 (= D189), G107 (= G276), K155 (= K320), D180 (= D347)
binding phosphate ion: D17 (= D187), D19 (= D189), S106 (= S275), K155 (= K320)
binding serine: G177 (= G344), T179 (≠ N346), R199 (≠ K363)

1l8lA Molecular basis for the local confomational rearrangement of human phosphoserine phosphatase (see paper)
33% identity, 48% coverage: 184:374/398 of query aligns to 14:210/222 of 1l8lA

query
sites
1l8lA

V

V

V

C

M

F

D
|
D

M
x
V

D
|
D

S

S

T

T

L

V

I

I

Q

R

V

E

E

E

V

G

I

I

D

D

E

E

L

L

A

A

R

K

V

I

A

C

G

G

V

V

G

E

E

D

Q

A

V

V

A

S

E

E

I

M

T

T

E

R

R

R

A

A

M

M

N

G

G

G

E

A

L

V

D

P

F

F

S

K

G

A

A

A

L

L

R

T

E

E

R

R

V

L

A

A

L

L

L

I

K

Q

G

P

L

S

K

R

A

E

E

Q

A

V

L

Q

E

R

Q

L

V

I

Y

A

R

E

N

Q

I

P

P

P

-

H

L

L

T

T

P

P

G

G

A

I

R

R

N

E

L

L

V

V

T

S

I

R

L

L

K

Q

R

E

L

R

G

N

F

V

K

Q

T

V

A

F

V

L

I

I

S

S

G
|
G

G

G

F

F

Q

R

F

S

F

I

T

V

D

E

R

H

L

V

K

A

S

S

D

K

L

L

G

N

L

I

D

P

Y

A

A

T

-

N

-

V

Y

F

A

A

N

N

G

R

L

L

E

K

I

F

V

Y

D

-

G

-

I

-

V

F

T

N

G

G

E

E

V

Y

A

A

G

G

-

F

-

D

-

E

-

T

-

Q

T

P

I

T

V

A

D

E

G

S

A

G

R

G

K
|
K

A

G

Q

K

L

V

L

I

E

K

E

F

I

L

A

-

G

-

K

K

E

E

G

K

I

F

T

H

L

F

D

K

Q

K

A

I

I

I

A

M

I

I

G

G

D
|
D

G
|
G

A

A

N
x
T

D
|
D

L

M

P

E

M

A

L

C

G

P

R

P

A

A

G

D

L

A

G

F

I

I

A

G

F

F

N

G

A

G

-

N

-

V

-

I

K

R

A

Q

R

Q

V

V

R

K

E

D

Q

N

A

A

D

K

F

W

H

Y

I

I

active site: D17 (= D187), V18 (≠ M188), D19 (= D189), G107 (= G276), K155 (= K320), D180 (= D347)
binding d-2-amino-3-phosphono-propionic acid: D17 (= D187), D19 (= D189), G107 (= G276), K155 (= K320), D176 (= D343), G177 (= G344), T179 (≠ N346)

6hyjB Psph human phosphoserine phosphatase (see paper)
33% identity, 48% coverage: 184:374/398 of query aligns to 17:213/223 of 6hyjB

query
sites
6hyjB

V

V

V

C

M

F

D
|
D

M

V

D
|
D

S

S

T

T

L

V

I

I

Q

R

V

E

E
|
E

V

G

I

I

D

D

E

E

L

L

A

A

R

K

V

I

A

C

G

G

V

V

G

E

E

D

Q

A

V

V

A

S

E

E

I

M

T

T

E

R

R

R

A

A

M

M

N

G

G

G

E

A

L

V

D

P

F

F

S

K

G

A

A

A

L

L

R

T

E

E

R

R

V

L

A

A

L

L

L

I

K

Q

G

P

L

S

K

R

A

E

E

Q

A

V

L

Q

E

R

Q

L

V

I

Y

A

R

E

N

Q

I

P

P

P

-

H

L

L

T

T

P

P

G

G

A

I

R

R

N

E

L

L

V

V

T

S

I

R

L

L

K

Q

R

E

L

R

G

N

F

V

K

Q

T

V

A

F

V

L

I

I

S

S

G

G

F

F

Q

R

F

S

F

I

T

V

D

E

R

H

L

V

K

A

S

S

D

K

L

L

G

N

L

I

D

P

Y

A

A

T

-

N

-

V

Y
x
F

A

A

N

N

G

R

L

L

E

K

I

F

V

Y

D

-

G

-

I

-

V

F

T

N

G

G

E

E

V

Y

A

A

G

G

-

F

-

D

-

E

-

T

-

Q

T

P

I

T

V

A

D

E

G

S

A

G

R

G

K

K

A

G

Q

K

L

V

L

I

E

K

E

L

I

L

A

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G

-

K

K

E

E

G
x
K

I

F

T

H

L

F

D

K

Q

K

A

I

I

I

A

M

I

I

G

G

D
|
D

G

G

A

A

N

T

D

D

L

M

P

E

M

A

L

C

G

P

R

P

A

A

G

D

L

A

G

F

I

I

A

G

F

F

N

G

A

G

-

N

-

V

-

I

K
x
R

A

Q

R

Q

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V

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K

E

D

Q

N

A

A

D

K

F

W

H

Y

I

I

binding calcium ion: D20 (= D187), D22 (= D189), D179 (= D343)
binding phosphoserine: F131 (≠ Y295), K168 (≠ G332)
binding serine: E29 (= E196), R202 (≠ K363)

P78330 Phosphoserine phosphatase; PSP; PSPase; L-3-phosphoserine phosphatase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Homo sapiens (Human) (see 4 papers)
33% identity, 48% coverage: 184:374/398 of query aligns to 17:213/225 of P78330

query
sites
P78330

V

V

V

C

M

F

D
|
D

M
x
V

D
|
D

S
|
S

T

T

L

V

I

I

Q

R

V

E

E
|
E

V

G

I

I

D
|
D

E

E

L

L

A
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A

R

K

V

I

A

C

G

G

V

V

G

E

E

D

Q

A

V

V

A

S

E

E

I

M

T

T

E

R

R

R

A

A

M
|
M

N
x
G

G

G

E

A

L

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D

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F

F

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K

G

A

A

A

L

L

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E

E

R
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R

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L

A

A

L

L

L

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G

P

L

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K

R

A

E

E

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A

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Q

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I

Y

A

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E

N

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H

L

L

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P

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G

A

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E

L

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L

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N

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S

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G

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F

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F

I

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E

R

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A

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S

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K

L

L

G

N

L

I

D

P

Y

A

A

T

-

N

-

V

Y

F

A

A

N
|
N

G

R

L

L

E

K

I

F

V

Y

D

-

G

-

I

-

V

F

T

N

G

G

E

E

V

Y

A

A

G

G

-

F

-

D

-

E

-

T

-

Q

T

P

I

T

V

A

D

E

G

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A

G

R

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K
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K

A

G

Q

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L

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L

I

E

K

E

L

I

L

A

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G

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K

K

E

E

G

K

I

F

T

H

L

F

D

K

Q

K

A

I

I

I

A

M

I

I

G

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D
|
D

G

G

A

A

N
x
T

D

D

L

M

P

E

M

A

L

C

G

P

R

P

A

A

G

D

L

A

G

F

I

I

A

G

F

F

N

G

A

G

-

N

-

V

-

I

K
x
R

A

Q

R

Q

V

V

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K

E

D

Q

N

A

A

D

K

F

W

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Y

I

I

D20 (= D187) binding Mg(2+)
DVD 20:22 (≠ DMD 187:189) binding L-serine
D22 (= D189) binding Mg(2+)
S23 (= S190) mutation to A: Reduces L-phosphoserine phosphatase activity by about 50%.; mutation to T: Reduces L-phosphoserine phosphatase activity by about 80%.
E29 (= E196) mutation to D: Reduces L-phosphoserine phosphatase activity by about 95%.; mutation to Q: Loss of L-phosphoserine phosphatase activity.
D32 (= D199) to N: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894035
A35 (= A202) to T: in PSPHD; decreased L-phosphoserine phosphatase activity
M52 (= M219) binding O-phospho-L-serine; to T: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894036
G53 (≠ N220) binding phosphate
R65 (= R232) mutation R->A,K: Loss of L-phosphoserine phosphatase activity.
SGG 109:111 (= SGG 275:277) binding L-serine; binding O-phospho-L-serine
N133 (= N297) mutation to A: Reduces L-phosphoserine phosphatase activity by about 75%.
K158 (= K320) binding L-serine; binding O-phospho-L-serine
D179 (= D343) binding Mg(2+)
T182 (≠ N346) binding O-phospho-L-serine; binding phosphate; mutation to S: Reduces L-phosphoserine phosphatase activity by about 99%.; mutation to V: Reduces L-phosphoserine phosphatase activity by about 25%.
R202 (≠ K363) mutation to A: Reduces L-phosphoserine phosphatase activity by about 99%.; mutation to K: Reduces L-phosphoserine phosphatase activity by about 95%.

6q6jB Human phosphoserine phosphatase with substrate analogue homo-cysteic acid (see paper)
33% identity, 48% coverage: 184:374/398 of query aligns to 13:209/217 of 6q6jB

query
sites
6q6jB

V

V

V

C

M

F

D
|
D

M
x
V

D
|
D

S

S

T

T

L

V

I

I

Q

R

V

E

E

E

V

G

I

I

D

D

E

E

L

L

A

A

R

K

V

I

A

C

G

G

V

V

G

E

E

D

Q

A

V

V

A

S

E

E

I

M

T

T

E

R

R

R

A

A

M

M

N

G

G

G

E

A

L

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D

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F
|
F

S

K

G

A

A

A

L

L

R

T

E

E

R

R

V

L

A

A

L

L

L

I

K

Q

G

P

L

S

K

R

A

E

E

Q

A

V

L

Q

E

R

Q

L

V

I

Y

A

R

E

N

Q

I

P

P

P

-

H

L

L

T

T

P

P

G

G

A

I

R

R

N

E

L

L

V

V

T

S

I

R

L

L

K

Q

R

E

L

R

G

N

F

V

K

Q

T

V

A

F

V

L

I

I

S
|
S

G
|
G

F

F

Q

R

F

S

F

I

T

V

D

E

R

H

L

V

K

A

S

S

D

K

L

L

G

N

L

I

D

P

Y

A

A

T

-

N

-

V

Y

F

A

A

N

N

G

R

L

L

E

K

I

F

V

Y

D

-

G

-

I

-

V

F

T

N

G

G

E

E

V

Y

A

A

G

G

-

F

-

D

-

E

-

T

-

Q

T

P

I

T

V

A

D

E

G

S

A

G

R

G

K
|
K

A

G

Q

K

L

V

L

I

E

K

E

L

I

L

A

-

G

-

K

K

E

E

G

K

I

F

T

H

L

F

D

K

Q

K

A

I

I

I

A

M

I

I

G

G

D
|
D

G

G

A

A

N
x
T

D

D