Structure of PDB 4hvo Chain A

Receptor sequence
>4hvoA (length=174) Species: 266264 (Cupriavidus metallidurans CH34) [Search protein sequence]
MLTYGAPFNFPRWIDEHAHLLKPPVGNRQVWQDSDFIVTVVGGPNHRTDY
HDDPLEEFFYQLRGNAYLNLWVDGRRERADLKEGDIFLLPPHVRHSPQRP
EAGSACLVIERQRPAGMLDGFEWYCDACGHLVHRVEVQLKSIVTDLPPLF
ESFYASEDKRRCPHCGQVHPGRAA
3D structure
PDB4hvo An Iron Reservoir to the Catalytic Metal: THE RUBREDOXIN IRON IN AN EXTRADIOL DIOXYGENASE.
ChainA
Resolution1.75 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.13.11.6: 3-hydroxyanthranilate 3,4-dioxygenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CU A H51 E57 H95 H51 E57 H95
BS02 FE2 A C125 C128 C162 C165 C125 C128 C162 C165
Gene Ontology
Molecular Function
GO:0000334 3-hydroxyanthranilate 3,4-dioxygenase activity
GO:0005506 iron ion binding
GO:0008198 ferrous iron binding
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
Biological Process
GO:0006569 tryptophan catabolic process
GO:0009435 NAD biosynthetic process
GO:0019363 pyridine nucleotide biosynthetic process
GO:0019805 quinolinate biosynthetic process
GO:0034354 'de novo' NAD biosynthetic process from tryptophan
GO:0043420 anthranilate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4hvo, PDBe:4hvo, PDBj:4hvo
PDBsum4hvo
PubMed25918158
UniProtQ1LCS4|3HAO_CUPMC 3-hydroxyanthranilate 3,4-dioxygenase (Gene Name=nbaC)

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