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6VI7

Probing extradiol dioxygenase mechanism in NAD(+) biosynthesis by viewing reaction cycle intermediates - a substrate bidentately bound structure

Functional Information from GO Data
ChainGOidnamespacecontents
A0000334molecular_function3-hydroxyanthranilate 3,4-dioxygenase activity
A0005506molecular_functioniron ion binding
A0006569biological_processL-tryptophan catabolic process
A0008198molecular_functionferrous iron binding
A0009435biological_processNAD+ biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0019363biological_processpyridine nucleotide biosynthetic process
A0019805biological_processquinolinate biosynthetic process
A0043420biological_processanthranilate metabolic process
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue 3HA A 201
ChainResidue
AVAL25
AGLU110
AILE142
AFE2202
AASN27
AVAL41
AARG47
AHIS51
AGLU57
APHE59
APRO97
AARG99

site_idAC2
Number of Residues4
Detailsbinding site for residue FE2 A 202
ChainResidue
AHIS51
AGLU57
AHIS95
A3HA201

site_idAC3
Number of Residues4
Detailsbinding site for residue FE2 A 203
ChainResidue
ACYS125
ACYS128
ACYS162
ACYS165

site_idAC4
Number of Residues6
Detailsbinding site for residue TRS A 204
ChainResidue
AVAL132
AHIS133
AASP158
ALYS159
AARG161
APRO163

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBinding site: {}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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