SitesBLAST

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)
45% identity, 56% coverage: 162:370/372 of query aligns to 180:387/409 of O53289

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O53289

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D185 (= D167) mutation to G: Completely abolishes enzymatic activity.; mutation to N: Completely abolishes enzymatic activity.
V186 (≠ M168) mutation to Q: Decreases enzymatic activity by 50%.
D187 (= D169) mutation to N: Decreases enzymatic activity by 15%.
S188 (= S170) mutation to A: No effect on enzymatic activity.
S273 (= S256) mutation to A: Completely abolishes enzymatic activity (PubMed:25521849). Decreases enzymatic activity by 60% (PubMed:25037224).
K318 (= K301) mutation to A: Decreases enzymatic activity by 50%.; mutation to E: Completely abolishes enzymatic activity.
D341 (= D324) 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 (= D328) 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)
40% identity, 55% coverage: 162:367/372 of query aligns to 5:209/210 of 1f5sA

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1f5sA

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active site: D10 (= D167), F11 (≠ M168), D12 (= D169), G99 (= G257), K143 (= K301), D170 (= D328)
binding magnesium ion: D10 (= D167), D12 (= D169), D166 (= D324)
binding phosphate ion: D10 (= D167), F11 (≠ M168), D12 (= D169), S98 (= S256), G99 (= G257), K143 (= K301)

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)
40% identity, 55% coverage: 162:367/372 of query aligns to 6:210/211 of Q58989

query
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Q58989

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D11 (= D167) active site, Nucleophile; binding Mg(2+); mutation to N: Loss of activity.
D13 (= D169) active site, Proton donor; binding Mg(2+)
E20 (= E176) binding substrate
R56 (= R212) binding substrate
SG 99:100 (= SG 256:257) binding substrate
K144 (= K301) binding substrate
D167 (= D324) binding Mg(2+)
N170 (= N327) binding substrate

1l7nA Transition state analogue of phosphoserine phosphatase (aluminum fluoride complex) (see paper)
40% identity, 55% coverage: 162:367/372 of query aligns to 4:208/209 of 1l7nA

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1l7nA

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active site: D9 (= D167), F10 (≠ M168), D11 (= D169), G98 (= G257), K142 (= K301), D169 (= D328)
binding aluminum fluoride: D9 (= D167), F10 (≠ M168), D11 (= D169), S97 (= S256), K142 (= K301)
binding tetrafluoroaluminate ion: D9 (= D167), F10 (≠ M168), D11 (= D169), S97 (= S256), G98 (= G257), K142 (= K301), N168 (= N327)
binding magnesium ion: D9 (= D167), D11 (= D169), D165 (= D324)

A0QJI1 Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Mycobacterium avium (strain 104) (see paper)
44% identity, 60% coverage: 148:370/372 of query aligns to 167:389/411 of A0QJI1

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A0QJI1

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D187 (= D167) binding Mg(2+)
D189 (= D169) binding Mg(2+)
D343 (= D324) binding Mg(2+)

8a21A Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with phenylimidazole (see paper)
44% identity, 60% coverage: 148:370/372 of query aligns to 163:385/396 of 8a21A

query
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8a21A

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R

-

L

L

Q

E

L

L

S

M

P

P

G

G

A

A

R

R

E

T

L

T

V

L

A

R

A

T

A

L

K

R

S

R

Q

L

G

G

V

Y

E

A

V

C

G

G

V

V

S

S

G

G

G
|
G

F

F

T

R

Q

R

F

I

T

I

R

E

H

P

L

L

Q

A

E

E

A

E

L

L

D

M

L

L

D

D

Y

Y

A

V

F

A

A

A

N

N

T

E

L

L

E

E

I

I

I

V

H

D

G

G

Q

T

I

L

T

T

G

G

Q

R

V

V

L

V

G

G

D

P

I

I

V

I

D

D

A

R

T

A

A

G

K

K

A

A

D

T

I

A

L

L

D

R

L

E

L

F

A

A

I

Q

G

R

L

A

G

G

T

V

D

P

A

M

G

A

H

Q

C

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

I

L

R

A

K

A

A

A

G

G

I

L

G

G

I

I

A

A

Y

F

H

N

A

A

K

K

A

P

V

A

V

L

R

R

A

E

Q

V

A

A

D

D

F

A

Q

S

I

L

R

S

Y

H

G

P

G

Y

L

L

D

D

T

T

A

V

A

L

A

F

Y

L

L

L

G

G

W

V

S

T

binding magnesium ion: D183 (= D167), D185 (= D169), D339 (= D324)
binding 4-phenyl-1h-imidazole: D185 (= D169), E192 (= E176), V193 (≠ C177), I194 (= I178), T211 (= T195), M215 (= M199), F221 (= F205), R228 (= R212), G273 (= G258)

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)
44% identity, 60% coverage: 148:370/372 of query aligns to 163:385/396 of 8a1zA

query
sites
8a1zA

L

V

D

D

V

V

A

A

V

V

S

E

P

D

L

Y

-

T

W

L

D

E

K

R

G

R

H

A

F

K

R

R

L

L

L

I

L

V

T

F

D
|
D

M

V

D
|
D

S

S

T

T

L

L

I

V

S

Q

I

G

E
|
E

C

V

I

I

D

E

E

M

L

L

A

A

E

A

H

K

L

A

G

G

L

A

R

E

R

G

Q

Q

V

V

A

A

I

I

T

T

E

D

R

A

S

A

M
|
M

A

R

G

G

E

E

L

L

D

D

F
|
F

Q

A

T

Q

S

S

L
|
L

R

Q

E

Q

R
|
R

V

V

R

A

L

T

L

L

A

A

G

G

T

L

P

P

A

A

S

T

S

V

I

I

D

D

T

E

I

V

I

A

R

G

E

Q

R

-

L

L

Q

E

L

L

S

M

P

P

G

G

A

A

R

R

E

T

L

T

V

L

A

R

A

T

A

L

K

R

S

R

Q

L

G

G

V

Y

E

A

V

C

G

G

V

V

S

S

G
|
G

G

G

F
|
F

T

R

Q

R

F

I

T

I

R

E

H

P

L

L

Q

A

E

E

A

E

L

L

D

M

L

L

D

D

Y

Y

A

V

F

A

A

A

N

N

T

E

L

L

E

E

I

I

I

V

H

D

G

G

Q

T

I

L

T

T

G

G

Q

R

V

V

L

V

G

G

D

P

I

I

V

I

D

D

A

R

T

A

A

G

K

K

A

A

D

T

I

A

L

L

D

R

L

E

L

F

A

A

I

Q

G

R

L

A

G

G

T

V

D

P

A

M

G

A

H

Q

C

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

I

L

R

A

K

A

A

A

G

G

I

L

G

G

I

I

A

A

Y

F

H

N

A

A

K

K

A

P

V

A

V

L

R

R

A

E

Q

V

A

A

D

D

F

A

Q

S

I

L

R

S

Y

H

G

P

G

Y

L

L

D

D

T

T

A

V

A

L

A

F

Y

L

L

L

G

G

W

V

S

T

binding 1-(2,4-dichlorophenyl)-3-oxidanyl-urea: D185 (= D169), E192 (= E176), M215 (= M199), F221 (= F205), L225 (= L209), R228 (= R212), G272 (= G257), F274 (= F259), D339 (= D324)
binding magnesium ion: D183 (= D167), D185 (= D169), D339 (= D324)

5jlpA Crystal structure of mycobacterium avium serb2 in complex with serine at act domain
44% identity, 60% coverage: 148:370/372 of query aligns to 163:385/396 of 5jlpA

query
sites
5jlpA

L

V

D

D

V

V

A

A

V

V

S

E

P

D

L

Y

-

T

W

L

D

E

K

R

G

R

H

A

F

K

R

R

L

L

L

I

L

V

T

F

D
|
D

M
x
V

D
|
D

S

S

T

T

L

L

I

V

S

Q

I

G

E

E

C

V

I

I

D

E

E

M

L

L

A

A

E

A

H

K

L

A

G

G

L

A

R

E

R

G

Q

Q

V

V

A

A

I

I

T

T

E

D

R

A

S

A

M

M

A

R

G

G

E

E

L

L

D

D

F

F

Q

A

T

Q

S

S

L

L

R

Q

E

Q

R

R

V

V

R

A

L

T

L

L

A

A

G

G

T

L

P

P

A

A

S

T

S

V

I

I

D

D

T

E

I

V

I

A

R

G

E

Q

R

-

L

L

Q

E

L

L

S

M

P

P

G

G

A

A

R

R

E

T

L

T

V

L

A

R

A

T

A

L

K

R

S

R

Q

L

G

G

V

Y

E

A

V

C

G

G

V

V

S

S

G
|
G

G

G

F

F

T

R

Q

R

F

I

T

I

R

E

H

P

L

L

Q

A

E

E

A

E

L

L

D

M

L

L

D

D

Y

Y

A

V

F

A

A

A

N

N

T

E

L

L

E

E

I

I

I

V

H

D

G

G

Q

T

I

L

T

T

G

G

Q

R

V

V

L

V

G

G

D

P

I

I

V

I

D

D

A

R

T

A

A

G

K
|
K

A

A

D

T

I

A

L

L

D

R

L

E

L

F

A

A

I

Q

G

R

L

A

G

G

T

V

D

P

A

M

G

A

H

Q

C

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

I

L

R

A

K

A

A

A

G

G

I

L

G

G

I

I

A

A

Y

F

H

N

A

A

K

K

A

P

V

A

V

L

R

R

A

E

Q

V

A

A

D

D

F

A

Q

S

I

L

R

S

Y

H

G

P

G

Y

L

L

D

D

T

T

A

V

A

L

A

F

Y

L

L

L

G

G

W

V

S

T

active site: D183 (= D167), V184 (≠ M168), D185 (= D169), G272 (= G257), K316 (= K301), D343 (= D328)
binding magnesium ion: D183 (= D167), D339 (= D324)

Sites not aligning to the query:

binding serine: 13, 14

1l7pA Substrate bound phosphoserine phosphatase complex structure (see paper)
40% identity, 55% coverage: 162:367/372 of query aligns to 3:207/208 of 1l7pA

query
sites
1l7pA

R

K

L

L

L

I

L

L

T

F

D
x
N

M
x
F

D
|
D

S

S

T

T

L

L

I

V

S

N

I

N

E
|
E

C

T

I

I

D

D

E

E

L

I

A

A

E

R

H

E

L

A

G

G

L

V

R

E

Q

E

V

V

A

K

I

I

T

T

E

K

R

E

S

A

M
|
M

A

E

G

G

E

K

L

L

D

N

F
|
F

Q

E

T

Q

S

S

L

L

R

R

E

K

R
|
R

V

V

R

S

L

L

A

K

G

D

T

L

P

P

A

I

S

E

S

K

I

V

D

E

T

K

I

A

I

I

R

K

E

-

R

R

L

I

Q

T

L

P

S

T

P

E

G

G

A

A

R

E

E

E

L

T

V

I

A

K

A

E

A

L

K

K

S

N

Q

R

G

G

V

Y

E

V

V

V

G

A

V

V

S
|
S

G
|
G

G

G

F

F

T

D

Q

I

F

A

T

V

R

N

H

K

L

I

Q

K

E

E

A

K

L

L

D

G

L

L

D

D

Y

Y

A

A

F

F

A

A

N

N

T

R

L

L

E

I

I

V

I

K

H

D

G

G

Q

K

I

L

T

T

G

G

Q

D

V

V

L

E

G

G

D

E

I

V

V

L

D

K

A

E

T

N

A

A

K
|
K

A

G

D

E

I

I

L

L

D

E

L

K

L

I

A

A

I

K

G

I

L

E

G

G

T

I

D

N

A

L

G

E

H

D

C

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

I

F

R

K

K

K

A

A

G

G

I

L

G

K

I

I

A

A

Y

F

H

C

A

A

K

K

A

P

V

I

V

L

R

K

A

E

Q

K

A

A

D

D

F

I

Q

C

I

I

R

E

Y

K

G

R

G

D

L

L

D

R

T

E

A

I

A

L

A

K

Y

Y

L

I

active site: N8 (≠ D167), F9 (≠ M168), D10 (= D169), G97 (= G257), K141 (= K301), D168 (= D328)
binding phosphoserine: N8 (≠ D167), F9 (≠ M168), D10 (= D169), E17 (= E176), M40 (= M199), F46 (= F205), R53 (= R212), S96 (= S256), G97 (= G257), K141 (= K301)

1l7oA Crystal structure of phosphoserine phosphatase in apo form (see paper)
38% identity, 55% coverage: 162:367/372 of query aligns to 3:199/200 of 1l7oA

query
sites
1l7oA

R

K

L

L

L

I

L

L

T

F

D

N

M

F

D

D

S

S

T

T

L

L

I

V

S

N

I

N

E

E

C

T

I

I

D

D

E

E

L

I

A

A

E

R

H

E

L

A

G

G

L

V

R

E

Q

E

V

V

A

K

I

I

T

T

E

-

R

-

S

-

M

-

A

-

G

-

E

-

L

-

D

N

F

F

Q

E

T

Q

S

S

L

L

R

R

E

K

R

R

V

V

R

S

L

L

A

K

G

D

T

L

P

P

A

I

S

E

S

K

I

V

D

E

T

K

I

A

I

I

R

K

E

-

R

R

L

I

Q

T

L

P

S

T

P

E

G

G

A

A

R

E

E

E

L

T

V

I

A

K

A

E

A

L

K

K

S

N

Q

R

G

G

V

Y

E

V

V

V

G

A

V

V

S

S

G

G

F

F

T

D

Q

I

F

A

T

V

R

N

H

K

L

I

Q

K

E

E

A

K

L

L

D

G

L

L

D

D

Y

Y

A

A

F

F

A

A

N

N

T

R

L

L

E

I

I

V

I

K

H

D

G

G

Q

K

I

L

T

T

G

G

Q

D

V

V

L

E

G

G

D

E

I

V

V

L

D

K

A

E

T

N

A

A

K

K

A

G

D

E

I

I

L

L

D

E

L

K

L

I

A

A

I

K

G

I

L

E

G

G

T

I

D

N

A

L

G

E

H

D

C

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

I

F

R

K

K

K

A

A

G

G

I

L

G

K

I

I

A

A

Y

F

H

C

A

A

K

K

A

P

V

I

V

L

R

K

A

E

Q

K

A

A

D

D

F

I

Q
x
C

I

I

R
x
E

Y

K

G

R

G

D

L

L

D

R

T

E

A

I

A

L

A

K

Y

Y

L

I

binding zinc ion: C186 (≠ Q354), E188 (≠ R356)

3m1yC Crystal structure of a phosphoserine phosphatase (serb) from helicobacter pylori
38% identity, 51% coverage: 162:351/372 of query aligns to 4:191/208 of 3m1yC

query
sites
3m1yC

R

K

L

L

L

A

L

V

T

F

D
|
D

M
x
F

D
|
D

S

S

T

T

L

L

I

V

S

N

I

A

E

E

C

T

I

I

D

E

E

S

L

L

A

A

E

R

H

A

L

W

G

G

L

V

R

F

R

D

Q

E

V

V

A

K

A

T

I

I

T

T

E

L

R

K

S

A

M

M

A

N

G

G

E

T

L

-

D

D

F

F

Q

H

T

K

S

S

L

L

R

I

E

L

R

R

V

V

R

S

L

K

L

L

A

K

G

N

T

M

P

P

A

L

S

K

S

L

I

A

D

K

T

E

I

V

I

C

R

-

E

E

R

S

L

L

Q

P

L

L

S

F

P

E

G

G

A

A

R

L

E

E

L

L

V

V

A

S

A

A

A

L

K

K

S

E

Q

K

G

N

V

Y

E

K

V

V

G

V

V

C

V

F

S

S

G
|
G

G

G

F

F

T

D

Q

L

F

A

T

T

R

N

H

H

L

Y

Q

R

E

D

A

L

L

L

D

H

L

L

D

D

Y

A

A

A

F

F

A

S

N

N

T

T

L

L

E

I

I

V

I

E

H

N

G

D

Q

A

I

L

T

N

G

G

Q

L

V

V

L

T

G

G

D

H

I

M

V

M

D

F

A

S

T

H

A

S

K
|
K

A

G

D

E

I

M

L

L

D

L

L

V

L

L

A

Q

I

R

G

L

L

L

G

N

T

I

D

S

A

K

G

T

H

N

C

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

I

F

R

K

K

H

A

A

G

H

I

I

G

K

I

I

A

A

Y

F

H

N

A

A

K

K

A

E

V

V

V

L

R

K

A

Q

Q

H

A

A

active site: D9 (= D167), F10 (≠ M168), D11 (= D169), G97 (= G257), K141 (= K301), D168 (= D328)
binding magnesium ion: D9 (= D167), D11 (= D169), D164 (= D324)

6q6jB Human phosphoserine phosphatase with substrate analogue homo-cysteic acid (see paper)
31% identity, 49% coverage: 167:350/372 of query aligns to 16:200/217 of 6q6jB

query
sites
6q6jB

D
|
D

M
x
V

D
|
D

S

S

T

T

L

V

I

I

S

R

I

E

E

E

C

G

I

I

D

D

E

E

L

L

A

A

E

K

H

I

L

C

G

G

L

V

R

E

R

D

Q

A

V

V

A

S

A

E

I

M

T

T

E

R

R

R

S

A

M

M

A

G

G

G

E

A

L

V

D

P

F
|
F

Q

K

T

A

S

A

L

L

R

T

E

E

R

R

V

L

R

A

L

L

L

I

A

Q

G

P

T

S

P

R

A

E

S

Q

S

V

I

Q

D

R

T

L

I

I

I

A

R

E

E

Q

R

P

L

P

Q

H

L

L

S

T

P

P

G

G

A

I

R

R

E

E

L

L

V

V

A

S

A

R

A

L

K

Q

S

E

Q

R

G

N

V

V

E

Q

V

V

G

F

V

L

V

I

S
|
S

G
|
G

F

F

T

R

Q

S

F

I

T

V

R

E

H

H

L

V

Q

A

E

S

A

K

L

L

D

N

L

I

-

P

-

A

D

T

Y

N

A

V

F

F

A

A

N

N

T

R

L

L

E

K

I

F

-

Y

I

F

H

N

G

G

Q

E

I

Y

T

A

G

G

-

F

Q

D

V

E

L

T

G

Q

D

P

I

T

V

A

D

E

A

S

T

G

A

G

K
|
K

A

G

D

K

I

V

L

I

D

K

L

L

A

K

I

E

G

K

L

F

G

H

T

F

D

K

A

-

G

-

H

K

C

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

I

C

R

P

K

P

A

A

G

D

I

A

G

F

I

I

A

G

Y

F

H

G

A

G

K

N

A

-

V

V

V

I

R

R

A

Q

Q

Q

binding calcium ion: D16 (= D167), D18 (= D169), D175 (= D324)
binding (2~{S})-2-azanyl-4-sulfo-butanoic acid: D16 (= D167), V17 (≠ M168), D18 (= D169), F54 (= F205), S105 (= S256), G106 (= G257), G107 (= G258), K154 (= K301), T178 (≠ N327)

6hyjB Psph human phosphoserine phosphatase (see paper)
31% identity, 49% coverage: 167:350/372 of query aligns to 20:204/223 of 6hyjB

query
sites
6hyjB

D
|
D

M

V

D
|
D

S

S

T

T

L

V

I

I

S

R

I

E

E
|
E

C

G

I

I

D

D

E

E

L

L

A

A

E

K

H

I

L

C

G

G

L

V

R

E

R

D

Q

A

V

V

A

S

A

E

I

M

T

T

E

R

R

R

S

A

M

M

A

G

G

G

E

A

L

V

D

P

F

F

Q

K

T

A

S

A

L

L

R

T

E

E

R

R

V

L

R

A

L

L

L

I

A

Q

G

P

T

S

P

R

A

E

S

Q

S

V

I

Q

D

R

T

L

I

I

I

A

R

E

E

Q

R

P

L

P

Q

H

L

L

S

T

P

P

G

G

A

I

R

R

E

E

L

L

V

V

A

S

A

R

A

L

K

Q

S

E

Q

R

G

N

V

V

E

Q

V

V

G

F

V

L

V

I

S

S

G

G

F

F

T

R

Q

S

F

I

T

V

R

E

H

H

L

V

Q

A

E

S

A

K

L

L

D

N

L

I

-

P

-

A

D

T

Y

N

A

V

F
|
F

A

A

N

N

T

R

L

L

E

K

I

F

-

Y

I

F

H

N

G

G

Q

E

I

Y

T

A

G

G

-

F

Q

D

V

E

L

T

G

Q

D

P

I

T

V

A

D

E

A

S

T

G

A

G

K

K

A

G

D

K

I

V

L

I

D

K

L

L

A

K

I

E

G
x
K

L

F

G

H

T

F

D

K

A

-

G

-

H

K

C

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

I

C

R

P

K

P

A

A

G

D

I

A

G

F

I

I

A

G

Y

F

H

G

A

G

K

N

A

-

V

V

V

I

R
|
R

A

Q

Q

Q

binding calcium ion: D20 (= D167), D22 (= D169), D179 (= D324)
binding phosphoserine: F131 (= F276), K168 (≠ G311)
binding serine: E29 (= E176), R202 (= R348)

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, 49% coverage: 167:350/372 of query aligns to 20:204/225 of P78330

query
sites
P78330

D
|
D

M
x
V

D
|
D

S
|
S

T

T

L

V

I

I

S

R

I

E

E
|
E

C

G

I

I

D
|
D

E

E

L

L

A
|
A

E

K

H

I

L

C

G

G

L

V

R

E

R

D

Q

A

V

V

A

S

A

E

I

M

T

T

E

R

R

R

S

A

M
|
M

A
x
G

G

G

E

A

L

V

D

P

F

F

Q

K

T

A

S

A

L

L

R

T

E

E

R
|
R

V

L

R

A

L

L

L

I

A

Q

G

P

T

S

P

R

A

E

S

Q

S

V

I

Q

D

R

T

L

I

I

I

A

R

E

E

Q

R

P

L

P

Q

H

L

L

S

T

P

P

G

G

A

I

R

R

E

E

L

L

V

V

A

S

A

R

A

L

K

Q

S

E

Q

R

G

N

V

V

E

Q

V

V

G

F

V

L

V

I

S
|
S

G
|
G

F

F

T

R

Q

S

F

I

T

V

R

E

H

H

L

V

Q

A

E

S

A

K

L

L

D

N

L

I

-

P

-

A

D

T

Y

N

A

V

F

F

A

A

N
|
N

T

R

L

L

E

K

I

F

-

Y

I

F

H

N

G

G

Q

E

I

Y

T

A

G

G

-

F

Q

D

V

E

L

T

G

Q

D

P

I

T

V

A

D

E

A

S

T

G

A

G

K
|
K

A

G

D

K

I

V

L

I

D

K

L

L

A

K

I

E

G

K

L

F

G

H

T

F

D

K

A

-

G

-

H

K

C

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

I

C

R

P

K

P

A

A

G

D

I

A

G

F

I

I

A

G

Y

F

H

G

A

G

K

N

A

-

V

V

V

I

R
|
R

A

Q

Q

Q

D20 (= D167) binding Mg(2+)
DVD 20:22 (≠ DMD 167:169) binding L-serine
D22 (= D169) binding Mg(2+)
S23 (= S170) mutation to A: Reduces L-phosphoserine phosphatase activity by about 50%.; mutation to T: Reduces L-phosphoserine phosphatase activity by about 80%.
E29 (= E176) mutation to D: Reduces L-phosphoserine phosphatase activity by about 95%.; mutation to Q: Loss of L-phosphoserine phosphatase activity.
D32 (= D179) to N: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894035
A35 (= A182) to T: in PSPHD; decreased L-phosphoserine phosphatase activity
M52 (= M199) binding O-phospho-L-serine; to T: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894036
G53 (≠ A200) binding phosphate
R65 (= R212) mutation R->A,K: Loss of L-phosphoserine phosphatase activity.
SGG 109:111 (= SGG 256:258) binding L-serine; binding O-phospho-L-serine
N133 (= N278) mutation to A: Reduces L-phosphoserine phosphatase activity by about 75%.
K158 (= K301) binding L-serine; binding O-phospho-L-serine
D179 (= D324) binding Mg(2+)
T182 (≠ N327) 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 (= R348) mutation to A: Reduces L-phosphoserine phosphatase activity by about 99%.; mutation to K: Reduces L-phosphoserine phosphatase activity by about 95%.

6hyyA Human phosphoserine phosphatase with serine and phosphate (see paper)
31% identity, 49% coverage: 167:350/372 of query aligns to 16:200/221 of 6hyyA

query
sites
6hyyA

D
|
D

M
x
V

D
|
D

S

S

T

T

L

V

I

I

S

R

I

E

E

E

C

G

I

I

D

D

E

E

L

L

A

A

E

K

H

I

L

C

G

G

L

V

R

E

R

D

Q

A

V

V

A

S

A

E

I

M

T

T

E

R

R

R

S

A

M

M

A

G

G

G

E

A

L

V

D

P

F

F

Q

K

T

A

S

A

L

L

R

T

E

E

R

R

V

L

R

A

L

L

L

I

A

Q

G

P

T

S

P

R

A

E

S

Q

S

V

I

Q

D

R

T

L

I

I

I

A

R

E

E

Q

R

P

L

P

Q

H

L

L

S

T

P

P

G

G

A

I

R

R

E

E

L

L

V

V

A

S

A

R

A

L

K

Q

S

E

Q

R

G

N

V

V

E

Q

V

V

G

F

V

L

V

I

S
|
S

G
|
G

G

G

F

F

T

R

Q

S

F

I

T

V

R

E

H

H

L

V

Q

A

E

S

A

K

L

L

D

N

L

I

-

P

-

A

D

T

Y

N

A

V

F

F

A

A

N

N

T

R

L

L

E

K

I

F

-

Y

I

F

H

N

G

G

Q

E

I

Y

T

A

G

G

-

F

Q

D

V

E

L

T

G

Q

D

P

I

T

V

A

D

E

A

S

T

G

A

G

K
|
K

A

G

D

K

I

V

L

I

D

K

L

L

A

K

I

E

G

K

L

F

G

H

T

F

D

K

A

-

G

-

H

K

C

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

I

C

R

P

K

P

A

A

G

D

I

A

G

F

I

I

A

G

Y

F

H

G

A

G

K

N

A

-

V

V

V

I

R

R

A

Q

Q

Q

binding magnesium ion: D16 (= D167), D18 (= D169), D175 (= D324)
binding serine: D16 (= D167), V17 (≠ M168), D18 (= D169), S105 (= S256), G106 (= G257), K154 (= K301)

1l8oA Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase (see paper)
31% identity, 49% coverage: 167:350/372 of query aligns to 17:201/222 of 1l8oA

query
sites
1l8oA

D
|
D

M
x
V

D
|
D

S

S

T

T

L

V

I

I

S

R

I

E

E

E

C

G

I

I

D

D

E

E

L

L

A

A

E

K

H

I

L

C

G

G

L

V

R

E

R

D

Q

A

V

V

A

S

A

E

I

M

T

T

E

R

R

R

S

A

M

M

A

G

G

G

E

A

L

V

D

P

F

F

Q

K

T

A

S

A

L

L

R

T

E

E

R

R

V

L

R

A

L

L

L

I

A

Q

G

P

T

S

P

R

A

E

S

Q

S

V

I

Q

D

R

T

L

I

I

I

A

R

E

E

Q

R

P

L

P

Q

H

L

L

S

T

P

P

G

G

A

I

R

R

E

E

L

L

V

V

A

S

A

R

A

L

K

Q

S

E

Q

R

G

N

V

V

E

Q

V

V

G

F

V

L

V

I

S
|
S

G
|
G

G

G

F

F

T

R

Q

S

F

I

T

V

R

E

H

H

L

V

Q

A

E

S

A

K

L

L

D

N

L

I

-

P

-

A

D

T

Y

N

A

V

F

F

A

A

N

N

T

R

L

L

E

K

I

F

-

Y

I

F

H

N

G

G

Q

E

I

Y

T

A

G

G

-

F

Q

D

V

E

L

T

G

Q

D

P

I

T

V

A

D

E

A

S

T

G

A

G

K
|
K

A

G

D

K

I

V

L

I

D

K

L

F

L

L

A

K

I

E

G

K

L

F

G

H

T

F

D

K

A

-

G

-

H

K

C

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

I

C

R

P

K

P

A

A

G

D

I

A

G

F

I

I

A

G

Y

F

H

G

A

G

K

N

A

-

V

V

V

I

R
|
R

A

Q

Q

Q

active site: D17 (= D167), V18 (≠ M168), D19 (= D169), G107 (= G257), K155 (= K301), D180 (= D328)
binding phosphate ion: D17 (= D167), D19 (= D169), S106 (= S256), K155 (= K301)
binding serine: G177 (= G325), T179 (≠ N327), R199 (= R348)

1l8lA Molecular basis for the local confomational rearrangement of human phosphoserine phosphatase (see paper)
31% identity, 49% coverage: 167:350/372 of query aligns to 17:201/222 of 1l8lA

query
sites
1l8lA

D
|
D

M
x
V

D
|
D

S

S

T

T

L

V

I

I

S

R

I

E

E

E

C

G

I

I

D

D

E

E

L

L

A

A

E

K

H

I

L

C

G

G

L

V

R

E

R

D

Q

A

V

V

A

S

A

E

I

M

T

T

E

R

R

R

S

A

M

M

A

G

G

G

E

A

L

V

D

P

F

F

Q

K

T

A

S

A

L

L

R

T

E

E

R

R

V

L

R

A

L

L

L

I

A

Q

G

P

T

S

P

R

A

E

S

Q

S

V

I

Q

D

R

T

L

I

I

I

A

R

E

E

Q

R

P

L

P

Q

H

L

L

S

T

P

P

G

G

A

I

R

R

E

E

L

L

V

V

A

S

A

R

A

L

K

Q

S

E

Q

R

G

N

V

V

E

Q

V

V

G

F

V

L

V

I

S

S

G
|
G

G

G

F

F

T

R

Q

S

F

I

T

V

R

E

H

H

L

V

Q

A

E

S

A

K

L

L

D

N

L

I

-

P

-

A

D

T

Y

N

A

V

F

F

A

A

N

N

T

R

L

L

E

K

I

F

-

Y

I

F

H

N

G

G

Q

E

I

Y

T

A

G

G

-

F

Q

D

V

E

L

T

G

Q

D

P

I

T

V

A

D

E

A

S

T

G

A

G

K
|
K

A

G

D

K

I

V

L

I

D

K

L

F

L

L

A

K

I

E

G

K

L

F

G

H

T

F

D

K

A

-

G

-

H

K

C

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

I

C

R

P

K

P

A

A

G

D

I

A

G

F

I

I

A

G

Y

F

H

G

A

G

K

N

A

-

V

V

V

I

R

R

A

Q

Q

Q

active site: D17 (= D167), V18 (≠ M168), D19 (= D169), G107 (= G257), K155 (= K301), D180 (= D328)
binding d-2-amino-3-phosphono-propionic acid: D17 (= D167), D19 (= D169), G107 (= G257), K155 (= K301), D176 (= D324), G177 (= G325), T179 (≠ N327)

4ap9A Crystal structure of phosphoserine phosphatase from t.Onnurineus in complex with ndsb-201 (see paper)
28% identity, 51% coverage: 151:340/372 of query aligns to 2:174/200 of 4ap9A

query
sites
4ap9A

A

A

V

M

S

D

P

P

L

Q

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active site: D15 (= D167), I16 (≠ M168), E17 (≠ D169), G103 (= G257), K141 (= K301), D162 (= D328)
binding 3-pyridinium-1-ylpropane-1-sulfonate: R31 (≠ E183), I32 (≠ H184), T33 (≠ L185), L46 (≠ M199), W52 (≠ F205), D140 (≠ A300), K141 (= K301), Y160 (≠ A326), A161 (≠ N327)

6iuyA Structure of dsgpdh of dunaliella salina (see paper)
30% identity, 31% coverage: 167:280/372 of query aligns to 20:137/585 of 6iuyA

query
sites
6iuyA

D
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D

M

V

D
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D

S

R

T

T

L

V

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T

S

T

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D

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D

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E

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T

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N

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binding magnesium ion: D20 (= D167), D22 (= D169)

Sites not aligning to the query:

binding magnesium ion: 175
binding nicotinamide-adenine-dinucleotide: 233, 234, 235, 236, 268, 290, 321, 324, 349, 381, 382, 497, 529, 530, 532

Query Sequence

>WP_012536111.1 NCBI__GCF_000021485.1:WP_012536111.1
MSSTRLAILSPAARGPMSLPASMGQLVAEVESHQEVWGCWLQSWDMPVTVGEIAPFLDEL
SRQALHQEREVIWAPMSSAESAVRLVLHGAARPEALRRALTTLHLQNLMPGRVLHCQGDD
LALILHGSRGPLSAVNHRLIEALEGITLDVAVSPLWDKGHFRLLLTDMDSTLISIECIDE
LAEHLGLRRQVAAITERSMAGELDFQTSLRERVRLLAGTPASSIDTIIRERLQLSPGARE
LVAAAKSQGVEVGVVSGGFTQFTRHLQEALDLDYAFANTLEIIHGQITGQVLGDIVDATA
KADILDLLAIGLGTDAGHCIAIGDGANDLPMIRKAGIGIAYHAKAVVRAQADFQIRYGGL
DTAAAYLGWSTA

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