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5BZZ

Crystal structure of human phosphatase PTEN in its reduced state

Functional Information from GO Data
ChainGOidnamespacecontents
A0016311biological_processdephosphorylation
A0016791molecular_functionphosphatase activity
B0016311biological_processdephosphorylation
B0016791molecular_functionphosphatase activity
C0016311biological_processdephosphorylation
C0016791molecular_functionphosphatase activity
D0016311biological_processdephosphorylation
D0016791molecular_functionphosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue TLA A 401
ChainResidue
AASP92
AHIS93
ACYS124
ALYS125
AALA126
AGLY129
AARG130
AGLN171

site_idAC2
Number of Residues8
Detailsbinding site for residue TLA B 401
ChainResidue
BHIS93
BCYS124
BLYS125
BALA126
BGLY129
BARG130
BGLN171
BASP92

site_idAC3
Number of Residues9
Detailsbinding site for residue TLA C 401
ChainResidue
CASP92
CHIS93
CCYS124
CLYS125
CALA126
CGLY129
CARG130
CGLN171
CHOH507

site_idAC4
Number of Residues9
Detailsbinding site for residue TLA D 401
ChainResidue
DASP92
DHIS93
DCYS124
DLYS125
DALA126
DGLY129
DARG130
DGLN171
DHOH560

Functional Information from PROSITE/UniProt
site_idPS00383
Number of Residues11
DetailsTYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. IHCkaGkgRTG
ChainResidueDetails
AILE122-GLY132

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues684
DetailsDomain: {"description":"Phosphatase tensin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00590","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues40
DetailsRegion: {"description":"Required for interaction with NOP53","evidences":[{"source":"PubMed","id":"15355975","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsActive site: {"description":"Phosphocysteine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00590","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"26166433","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine; by FRK","evidences":[{"source":"PubMed","id":"19345329","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 456
ChainResidueDetails
AASP92proton shuttle (general acid/base)
ACYS124covalent catalysis
AARG130transition state stabiliser

site_idMCSA2
Number of Residues3
DetailsM-CSA 456
ChainResidueDetails
BASP92proton shuttle (general acid/base)
BCYS124covalent catalysis
BARG130transition state stabiliser

site_idMCSA3
Number of Residues3
DetailsM-CSA 456
ChainResidueDetails
CASP92proton shuttle (general acid/base)
CCYS124covalent catalysis
CARG130transition state stabiliser

site_idMCSA4
Number of Residues3
DetailsM-CSA 456
ChainResidueDetails
DASP92proton shuttle (general acid/base)
DCYS124covalent catalysis
DARG130transition state stabiliser

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PDB entries from 2026-01-14

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