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5GTJ

CRYSTAL STRUCTURE OF CATALYTICALLY ACTIVE FORM OF HUMAN DUSP26

Functional Information from GO Data
ChainGOidnamespacecontents
A0006470biological_processprotein dephosphorylation
A0008138molecular_functionprotein tyrosine/serine/threonine phosphatase activity
A0016311biological_processdephosphorylation
B0006470biological_processprotein dephosphorylation
B0008138molecular_functionprotein tyrosine/serine/threonine phosphatase activity
B0016311biological_processdephosphorylation
C0006470biological_processprotein dephosphorylation
C0008138molecular_functionprotein tyrosine/serine/threonine phosphatase activity
C0016311biological_processdephosphorylation
D0006470biological_processprotein dephosphorylation
D0008138molecular_functionprotein tyrosine/serine/threonine phosphatase activity
D0016311biological_processdephosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue PO4 A 301
ChainResidue
AASP120
ASER152
AALA153
AVAL154
AGLY155
AVAL156
ASER157
AARG158
AHOH440

site_idAC2
Number of Residues9
Detailsbinding site for residue PO4 B 301
ChainResidue
BASP120
BSER152
BALA153
BVAL154
BGLY155
BVAL156
BSER157
BARG158
BHOH440

site_idAC3
Number of Residues9
Detailsbinding site for residue PO4 C 301
ChainResidue
CASP120
CSER152
CALA153
CVAL154
CGLY155
CVAL156
CSER157
CARG158
CHOH467

site_idAC4
Number of Residues9
Detailsbinding site for residue PO4 D 301
ChainResidue
DASP120
DSER152
DALA153
DVAL154
DGLY155
DVAL156
DSER157
DARG158
DHOH447

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues588
DetailsDomain: {"description":"Tyrosine-protein phosphatase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00160","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Phosphocysteine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00160","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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