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2BZL

CRYSTAL STRUCTURE OF THE HUMAN PROTEIN TYROSINE PHOSPHATASE N14 AT 1. 65 A RESOLUTION

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 Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A2185
ChainResidue
AARG1021
ALYS1025
AARG1045
AHOH2125

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A2186
ChainResidue
AHIS1030
ASER1031
ASER1032
AHOH2244

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A2187
ChainResidue
ASER1122
AGLY1126
AARG1127
AGLN1169
AHOH2225
ACYS1121

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A2188
ChainResidue
APRO917
ALYS918
ALYS919

Functional Information from PROSITE/UniProt
site_idPS00383
Number of Residues11
DetailsTYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. VHCsaGvgRTG
ChainResidueDetails
AVAL1119-GLY1129

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Phosphocysteine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00160","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10044","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1ytw
ChainResidueDetails
AGLU1013
AHIS1120
AASP1079
AARG1127
ACYS1121
ATHR1128

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ytw
ChainResidueDetails
AARG1127
AASP1079
ACYS1121
ATHR1128

247536

PDB entries from 2026-01-14

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