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2I1Y

Crystal structure of the phosphatase domain of human PTP IA-2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004725molecular_functionprotein tyrosine phosphatase activity
A0006470biological_processprotein dephosphorylation
A0016311biological_processdephosphorylation
A0030141cellular_componentsecretory granule
B0004725molecular_functionprotein tyrosine phosphatase activity
B0006470biological_processprotein dephosphorylation
B0016311biological_processdephosphorylation
B0030141cellular_componentsecretory granule
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 3288
ChainResidue
ALEU926
AMET929
AALA930
AILE973

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 3287
ChainResidue
BLEU926
BMET929
BVAL970
BILE973

Functional Information from PROSITE/UniProt
site_idPS00383
Number of Residues11
DetailsTYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. VHCsdGagRTG
ChainResidueDetails
AVAL907-GLY917

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues520
DetailsDomain: {"description":"Tyrosine-protein phosphatase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00160","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)","evidences":[{"source":"PubMed","id":"16622421","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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