Structure of PDB 1gqh Chain A Binding Site BS02

Receptor Information

>1gqh Chain A (length=341) Species: 34381 (Aspergillus japonicus)

TSSLIVEDAPDHVRPYVIRHYSHARAVTVDTQLYRFYVTGPSSGYAFTLM
GTNAPHSDALGVLPHIHQKHYENFYCNKGSFQLWAQSGNETQQTRVLSSG
DYGSVPRNVTHTFQIQDPDTEMTGVIVPGGFEDLFYYLGTNATDTTHTPY
IPSGPDSSTISTLQSFDVYAELSFTPRTDTVNGTAPANTVWHTGANALAS
TAGDPYFIANGWGPKYLNSQYGYQIVAPFVTATQAQDTNYTLSTISMSTT
PSTVTVPTWSFPGACAFQVQEGRVVVQIGDYAATELGSGDVAFIPGGVEF
KYYSEAYFSKVLFVSSGSDGLDQNLVNGGEEWSSVSFPADW

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: 1gqh Chain A Residue 1352

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1gqh Functional Analysis of the Copper-Dependent Quercetin 2,3-Dioxygenase.1.Ligand-Induced Coordination Changes Probed by X-Ray Crystallography: Inhibition, Ordering Effect and Mechanistic Insights
• Resolution: 2.15 Å
• Binding residue (original residue number in PDB): H66 H68 E73 H112
• Binding residue (residue number reindexed from 1): H65 H67 E72 H111
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): H66 H68 E73 H112
• Catalytic site (residue number reindexed from 1): H65 H67 E72 H111
• Enzyme Commision number: 1.13.11.24: quercetin 2,3-dioxygenase.

Gene Ontology

Molecular Function

• GO:0008127 quercetin 2,3-dioxygenase activity
• GO:0046872 metal ion binding
• GO:0051213 dioxygenase activity

External links

• PDB: RCSB:1gqh, PDBe:1gqh, PDBj:1gqh
• PDBsum: 1gqh
• PubMed: 12069585
• UniProt: Q7SIC2|QDOI_ASPJA Quercetin 2,3-dioxygenase