Structure of PDB 1gqh Chain B

Receptor sequence
>1gqhB (length=334) Species: 34381 (Aspergillus japonicus) [Search protein sequence]
SSLIVEDAPDHVRPYVIRHYSHARAVTVDTQLYRFYVTGPSSGYAFTLMG
TNAPHSDALGVLPHIHQKHYENFYCNKGSFQLWAQSGNETQQTRVLSSGD
YGSVPRNVTHTFQIQDPDTEMTGVIVPGGFEDLFYYLGTNATDTTHTPYI
PTISTLQSFDVYAELSFTPRTDTVNGTAPANTVWHTGANALASTAGDPYF
IANGWGPKYLNSQYGYQIVAPFVTATQAQDTNYTLSTISMSTTPSTVTVP
TWSFPGACAFQVQEGRVVVQIGDYAATELGSGDVAFIPGGVEFKYYSEAY
FSKVLFVSSGSDGLDQNLVNGGEEWSSVSFPADW
3D structure
PDB1gqh 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
ChainB
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H66 H68 E73 H112
Catalytic site (residue number reindexed from 1) H64 H66 E71 H110
Enzyme Commision number 1.13.11.24: quercetin 2,3-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 KOJ B Y35 M51 T53 H66 H68 E73 H112 F114 M123 F132 F136 Y33 M49 T51 H64 H66 E71 H110 F112 M121 F130 F134
BS02 CU B H66 H68 E73 H112 H64 H66 E71 H110
Gene Ontology
Molecular Function
GO:0008127 quercetin 2,3-dioxygenase activity
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity

View graph for
Molecular Function
External links
PDB RCSB:1gqh, PDBe:1gqh, PDBj:1gqh
PDBsum1gqh
PubMed12069585
UniProtQ7SIC2|QDOI_ASPJA Quercetin 2,3-dioxygenase

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