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1ZC0

Crystal structure of human hematopoietic tyrosine phosphatase (HePTP) catalytic domain

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 PO4 A 436
ChainResidue
AASP236
AHOH578
ACYS270
ASER271
AALA272
AILE274
AGLY275
AARG276
AGLN314
AHOH438

Functional Information from PROSITE/UniProt
site_idPS00383
Number of Residues11
DetailsTYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. VHCsaGigRTG
ChainResidueDetails
AVAL268-GLY278

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
ACYS270

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING:
ChainResidueDetails
AASP236
ACYS270
AGLN314

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
ACYS270

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1ytw
ChainResidueDetails
AASP236
AHIS269
ATHR277
AARG276
ACYS270
AGLU178

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ytw
ChainResidueDetails
AASP236
AARG276
ATHR277
ACYS270

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PDB entries from 2024-09-11

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