Structure of PDB 1yfu Chain A Binding Site BS02

Receptor Information

>1yfu Chain A (length=174) Species: 119219 (Cupriavidus metallidurans)

MLTYGAPFNFPRWIDEHAHLLKPPVGNRQVWQDSDFIVTVVGGPNHRTDY
HDDPLEEFFYQLRGNAYLNLWVDGRRERADLKEGDIFLLPPHVRHSPQRP
EAGSACLVIERQRPAGMLDGFEWYCDACGHLVHRVEVQLKSIVTDLPPLF
ESFYASEDKRRCPHCGQVHPGRAA

Ligand information

• Ligand ID: FE
• InChI: InChI=1S/Fe/q+3
• InChIKey: VTLYFUHAOXGGBS-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  CACTVS 3.341
  OpenEye OEToolkits 1.5.0: [Fe+3]
• Formula: Fe
• Name: FE (III) ION
• DrugBank: DB13949
• PDB chain: 1yfu Chain A Residue 301

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1yfu Structural Studies on 3-Hydroxyanthranilate-3,4-dioxygenase: The Catalytic Mechanism of a Complex Oxidation Involved in NAD Biosynthesis.
• Resolution: 1.9 Å
• Binding residue (original residue number in PDB): C125 C128 C162 C165
• Binding residue (residue number reindexed from 1): C125 C128 C162 C165
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 1.13.11.6: 3-hydroxyanthranilate 3,4-dioxygenase.

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

External links

• PDB: RCSB:1yfu, PDBe:1yfu, PDBj:1yfu
• PDBsum: 1yfu
• PubMed: 15909978
• UniProt: Q1LCS4|3HAO_CUPMC 3-hydroxyanthranilate 3,4-dioxygenase (Gene Name=nbaC)