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4RI5

Crystal structure of PTPN3 (PTPH1) D811E mutant in complex with metavanadate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004725molecular_functionprotein tyrosine phosphatase activity
A0006470biological_processprotein dephosphorylation
A0016311biological_processdephosphorylation
B0004725molecular_functionprotein tyrosine phosphatase activity
B0006470biological_processprotein dephosphorylation
B0016311biological_processdephosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1001
ChainResidue
AHIS812
AGLN886
AHOH1176
AHOH1260
AHOH1311
AHOH1374

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE VN4 A 1002
ChainResidue
AGLY845
AILE846
AGLY847
AARG848
AGLN886
AHOH1176
AHOH1384
ACYS842
ASER843
AALA844

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1001
ChainResidue
BTYR676
BHIS812
BGLN886
BHOH1247
BHOH1255
BHOH1415

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE VN4 B 1002
ChainResidue
BCYS842
BSER843
BALA844
BGLY845
BILE846
BGLY847
BARG848
BGLN886
BHOH1122
BHOH1415

Functional Information from PROSITE/UniProt
site_idPS00383
Number of Residues11
DetailsTYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. VHCsaGigRTG
ChainResidueDetails
AVAL840-GLY850

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Phosphocysteine intermediate => ECO:0000255|PROSITE-ProRule:PRU00160, ECO:0000255|PROSITE-ProRule:PRU10044
ChainResidueDetails
ACYS842
BCYS842

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLU811
ACYS842
AGLN886
BGLU811
BCYS842
BGLN886

218853

PDB entries from 2024-04-24

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