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6D0O

rdpA dioxygenase holoenzyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0000908molecular_functiontaurine dioxygenase activity
A0005737cellular_componentcytoplasm
A0006790biological_processsulfur compound metabolic process
A0016491molecular_functionoxidoreductase activity
A0019439biological_processobsolete aromatic compound catabolic process
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
B0000908molecular_functiontaurine dioxygenase activity
B0005737cellular_componentcytoplasm
B0006790biological_processsulfur compound metabolic process
B0016491molecular_functionoxidoreductase activity
B0019439biological_processobsolete aromatic compound catabolic process
B0046872molecular_functionmetal ion binding
B0051213molecular_functiondioxygenase activity
C0000908molecular_functiontaurine dioxygenase activity
C0005737cellular_componentcytoplasm
C0006790biological_processsulfur compound metabolic process
C0016491molecular_functionoxidoreductase activity
C0019439biological_processobsolete aromatic compound catabolic process
C0046872molecular_functionmetal ion binding
C0051213molecular_functiondioxygenase activity
D0000908molecular_functiontaurine dioxygenase activity
D0005737cellular_componentcytoplasm
D0006790biological_processsulfur compound metabolic process
D0016491molecular_functionoxidoreductase activity
D0019439biological_processobsolete aromatic compound catabolic process
D0046872molecular_functionmetal ion binding
D0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CO A 401
ChainResidue
AHIS111
AASP113
AHIS270
AAKG402
AHOH591

site_idAC2
Number of Residues9
Detailsbinding site for residue AKG A 402
ChainResidue
AARG281
AARG285
ACO401
AHOH502
AHOH591
AHIS111
AASP113
ATHR138
AHIS270

site_idAC3
Number of Residues4
Detailsbinding site for residue CO B 401
ChainResidue
BHIS111
BASP113
BHIS270
BAKG402

site_idAC4
Number of Residues10
Detailsbinding site for residue AKG B 402
ChainResidue
BHIS111
BASP113
BMET126
BTHR138
BHIS270
BARG281
BARG285
BCO401
BHOH612
BHOH642

site_idAC5
Number of Residues5
Detailsbinding site for residue CO C 401
ChainResidue
CHIS111
CASP113
CHIS270
CAKG402
CHOH542

site_idAC6
Number of Residues13
Detailsbinding site for residue AKG C 402
ChainResidue
CILE95
CGLY107
CHIS111
CASP113
CMET126
CTHR138
CHIS270
CALA272
CARG281
CARG285
CCO401
CHOH516
CHOH542

site_idAC7
Number of Residues5
Detailsbinding site for residue CO D 401
ChainResidue
DHIS111
DASP113
DHIS270
DAKG402
DHOH548

site_idAC8
Number of Residues13
Detailsbinding site for residue AKG D 402
ChainResidue
DILE95
DHIS111
DASP113
DMET126
DTHR138
DHIS270
DALA272
DARG281
DARG285
DCO401
DHOH509
DHOH548
DHOH579

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P37610
ChainResidueDetails
AHIS111
BTRP255
BHIS270
BARG281
CHIS111
CASP113
CTHR138
CTRP255
CHIS270
CARG281
DHIS111
AASP113
DASP113
DTHR138
DTRP255
DHIS270
DARG281
ATHR138
ATRP255
AHIS270
AARG281
BHIS111
BASP113
BTHR138

site_idSWS_FT_FI2
Number of Residues8
DetailsSITE: Contributes to enantiospecificity => ECO:0000303|PubMed:16731970
ChainResidueDetails
ATYR221
AARG285
BTYR221
BARG285
CTYR221
CARG285
DTYR221
DARG285

220113

PDB entries from 2024-05-22

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