Structure of PDB 4hvo Chain A Binding Site BS01

Receptor Information

>4hvo Chain A (length=174) Species: 266264 (Cupriavidus metallidurans CH34)

MLTYGAPFNFPRWIDEHAHLLKPPVGNRQVWQDSDFIVTVVGGPNHRTDY
HDDPLEEFFYQLRGNAYLNLWVDGRRERADLKEGDIFLLPPHVRHSPQRP
EAGSACLVIERQRPAGMLDGFEWYCDACGHLVHRVEVQLKSIVTDLPPLF
ESFYASEDKRRCPHCGQVHPGRAA

Ligand information

• Ligand ID: CU
• InChI: InChI=1S/Cu/q+2
• InChIKey: JPVYNHNXODAKFH-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Cu+2]
  CACTVS 3.341: [Cu++]
• Formula: Cu
• Name: COPPER (II) ION
• DrugBank: DB14552
• PDB chain: 4hvo Chain A Residue 300

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4hvo An Iron Reservoir to the Catalytic Metal: THE RUBREDOXIN IRON IN AN EXTRADIOL DIOXYGENASE.
• Resolution: 1.75 Å
• Binding residue (original residue number in PDB): H51 E57 H95
• Binding residue (residue number reindexed from 1): H51 E57 H95
• 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:4hvo, PDBe:4hvo, PDBj:4hvo
• PDBsum: 4hvo
• PubMed: 25918158
• UniProt: Q1LCS4|3HAO_CUPMC 3-hydroxyanthranilate 3,4-dioxygenase (Gene Name=nbaC)