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3D42

Crystal structure of HePTP in complex with a monophosphorylated Erk2 peptide

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 Residues10
DetailsBINDING SITE FOR RESIDUE TAR A 1
ChainResidue
AHIS59
ALEU328
APRO60
ALEU61
ATHR62
AALA65
ASER242
AALA243
AGLY244
AHIS324

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 2
ChainResidue
ATHR174
AGLN175
AARG177
AGLU181
ALYS182
ACYS183
AARG276

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by MAP2K1 and MAP2K2 => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
BTHR183

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by MAP2K1 and MAP2K2 => ECO:0000269|PubMed:19053285, ECO:0000269|PubMed:19494114, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
BPTR185
ASER270
AGLN314

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:19060905
ChainResidueDetails
BTHR188

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

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PDB entries from 2024-09-11

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