Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1ZVF

The crystal structure of 3-hydroxyanthranilate 3,4-dioxygenase from Saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0000334molecular_function3-hydroxyanthranilate 3,4-dioxygenase activity
A0005506molecular_functioniron ion binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
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
A0034354biological_process'de novo' NAD+ biosynthetic process from L-tryptophan
A0043420biological_processanthranilate metabolic process
A0046872molecular_functionmetal ion binding
A0046874biological_processquinolinate metabolic process
A0051213molecular_functiondioxygenase activity
B0000334molecular_function3-hydroxyanthranilate 3,4-dioxygenase activity
B0005506molecular_functioniron ion binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0006569biological_processL-tryptophan catabolic process
B0008198molecular_functionferrous iron binding
B0009435biological_processNAD+ biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0019363biological_processpyridine nucleotide biosynthetic process
B0019805biological_processquinolinate biosynthetic process
B0034354biological_process'de novo' NAD+ biosynthetic process from L-tryptophan
B0043420biological_processanthranilate metabolic process
B0046872molecular_functionmetal ion binding
B0046874biological_processquinolinate metabolic process
B0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NI A 201
ChainResidue
AHIS49
AGLU55
AHIS97
AHOH205

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NI B 202
ChainResidue
BHIS49
BGLU55
BHIS97
BHOH205
BHOH206

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NI A 203
ChainResidue
ACYS126
ACYS129
ACYS163
ACYS166

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NI B 204
ChainResidue
BCYS126
BCYS129
BCYS163
BCYS166

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03019","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {}
ChainResidueDetails

249697

PDB entries from 2026-02-25

PDB statisticsPDBj update infoContact PDBjnumon