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2QDM

Crystal structure of the HePTP catalytic domain C270S/D236A/Q314A mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0004725molecular_functionprotein tyrosine phosphatase activity
A0006470biological_processprotein dephosphorylation
A0016311biological_processdephosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 340
ChainResidue
ASER270
ASER271
AALA272
AGLY273
AILE274
AGLY275
AARG276
AHOH344

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 341
ChainResidue
AGLN175
ASER271
AARG276
AHOH446
ATHR174

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Phosphocysteine intermediate => ECO:0000255|PROSITE-ProRule:PRU00160, ECO:0000255|PROSITE-ProRule:PRU10044, ECO:0000269|PubMed:9624114
ChainResidueDetails
ASER270

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING:
ChainResidueDetails
AALA236
ASER270
AALA314

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:10206983, ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR45

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:10206983
ChainResidueDetails
ASER72

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER89

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER122

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000250
ChainResidueDetails
ASER270

226707

PDB entries from 2024-10-30

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