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3V17

Crystal structure of the Fe(II)/alpha-ketoglutarate dependent taurine dioxygenase from Pseudomonas putida KT2440

Functional Information from GO Data
ChainGOidnamespacecontents
A0000907molecular_functionsulfonate dioxygenase activity
A0000908molecular_functiontaurine dioxygenase activity
A0003824molecular_functioncatalytic activity
A0005506molecular_functioniron ion binding
A0016491molecular_functionoxidoreductase activity
A0042802molecular_functionidentical protein binding
A0044273biological_processsulfur compound catabolic process
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
B0000907molecular_functionsulfonate dioxygenase activity
B0000908molecular_functiontaurine dioxygenase activity
B0003824molecular_functioncatalytic activity
B0005506molecular_functioniron ion binding
B0016491molecular_functionoxidoreductase activity
B0042802molecular_functionidentical protein binding
B0044273biological_processsulfur compound catabolic process
B0046872molecular_functionmetal ion binding
B0051213molecular_functiondioxygenase activity
C0000907molecular_functionsulfonate dioxygenase activity
C0000908molecular_functiontaurine dioxygenase activity
C0003824molecular_functioncatalytic activity
C0005506molecular_functioniron ion binding
C0016491molecular_functionoxidoreductase activity
C0042802molecular_functionidentical protein binding
C0044273biological_processsulfur compound catabolic process
C0046872molecular_functionmetal ion binding
C0051213molecular_functiondioxygenase activity
D0000907molecular_functionsulfonate dioxygenase activity
D0000908molecular_functiontaurine dioxygenase activity
D0003824molecular_functioncatalytic activity
D0005506molecular_functioniron ion binding
D0016491molecular_functionoxidoreductase activity
D0042802molecular_functionidentical protein binding
D0044273biological_processsulfur compound catabolic process
D0046872molecular_functionmetal ion binding
D0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE AKG A 279
ChainResidue
ALEU112
ATHR124
AHIS253
AARG264
AARG268

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE AKG C 279
ChainResidue
CHIS253
CARG264
CARG268
CASP99
CLEU112
CTHR124
CTRP246

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE AKG B 279
ChainResidue
BASN93
BTHR124
BHIS253
BALA255
BARG264

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE AKG D 279
ChainResidue
DLEU83
DASN93
DHIS97
DTHR124
DTRP246
DHIS253
DARG264
DMET266
DARG268
DHOH335

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues32
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P37610
ChainResidueDetails
AHIS68
CTYR71
CASN93
CHIS97
CASP99
CVAL100
CHIS253
CARG268
BHIS68
BTYR71
BASN93
ATYR71
BHIS97
BASP99
BVAL100
BHIS253
BARG268
DHIS68
DTYR71
DASN93
DHIS97
DASP99
AASN93
DVAL100
DHIS253
DARG268
AHIS97
AASP99
AVAL100
AHIS253
AARG268
CHIS68

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0007744|PDB:3V17
ChainResidueDetails
ATHR124
AARG264
CTHR124
CARG264
BTHR124
BARG264
DTHR124
DARG264

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PDB entries from 2024-07-24

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