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1BVH

SOLUTION STRUCTURE OF A LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003993molecular_functionacid phosphatase activity
A0004721molecular_functionphosphoprotein phosphatase activity
A0004725molecular_functionprotein tyrosine phosphatase activity
A0004726molecular_functionnon-membrane spanning protein tyrosine phosphatase activity
A0005737cellular_componentcytoplasm
A0006338biological_processchromatin remodeling
A0006470biological_processprotein dephosphorylation
A0016791molecular_functionphosphatase activity
A0030946molecular_functionprotein tyrosine phosphatase activity, metal-dependent
A0140793molecular_functionhistone H2AXY142 phosphatase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:8052313, ECO:0000269|PubMed:8132604, ECO:0000269|PubMed:8319676
ChainResidueDetails
ALEU13

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:8052313, ECO:0000269|PubMed:8319676
ChainResidueDetails
ASER19

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:8052313
ChainResidueDetails
APRO130

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:2644264
ChainResidueDetails
AGLU2

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P24666
ChainResidueDetails
ATYR132
AGLY133

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pnt
ChainResidueDetails
ACYS17
AARG18
AASP129
ACYS12

site_idMCSA1
Number of Residues6
DetailsM-CSA 462
ChainResidueDetails
ALEU13covalent catalysis
AILE16activator, electrostatic stabiliser
AARG18steric role
ASER19transition state stabiliser
APRO20activator, electrostatic stabiliser
APRO130proton shuttle (general acid/base)

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PDB entries from 2024-12-18

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