Structure of PDB 1yfx Chain A

Receptor sequence
>1yfxA (length=174) Species: 119219 (Cupriavidus metallidurans) [Search protein sequence]
MLTYGAPFNFPRWIDEHAHLLKPPVGNRQVWQDSDFIVTVVGGPNHRTDY
HDDPLEEFFYQLRGNAYLNLWVDGRRERADLKEGDIFLLPPHVRHSPQRP
EAGSACLVIERQRPAGMLDGFEWYCDACGHLVHRVEVQLKSIVTDLPPLF
ESFYASEDKRRCPHCGQVHPGRAA
3D structure
PDB1yfx Structural Studies on 3-Hydroxyanthranilate-3,4-dioxygenase: The Catalytic Mechanism of a Complex Oxidation Involved in NAD Biosynthesis.
ChainA
Resolution2.0 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 FE A H51 E57 H95 H51 E57 H95
BS02 FE A C125 C128 C162 C165 C125 C128 C162 C165
BS03 NO A R47 H51 H95 P97 R47 H51 H95 P97
BS04 4AA A V25 R47 H51 E57 F59 P97 R99 E110 I142 V25 R47 H51 E57 F59 P97 R99 E110 I142
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1yfx, PDBe:1yfx, PDBj:1yfx
PDBsum1yfx
PubMed15909978
UniProtQ1LCS4|3HAO_CUPMC 3-hydroxyanthranilate 3,4-dioxygenase (Gene Name=nbaC)

[Back to BioLiP]