Structure of PDB 1h1m Chain A

Receptor sequence
>1h1mA (length=344) Species: 34381 (Aspergillus japonicus) [Search protein sequence]
SSLIVEDAPDHVRPYVIRHYSHARAVTVDTQLYRFYVTGPSSGYAFTLMG
TNAPHSDALGVLPHIHQKHYENFYCNKGSFQLWAQSGNETQQTRVLSSGD
YGSVPRNVTHTFQIQDPDTEMTGVIVPGGFEDLFYYLGTNATDTTHTPYI
PSSSTTGPDSSTISTLQSFDVYAELSFTPRTDTVNGTAPANTVWHTGANA
LASTAGDPYFIANGWGPKYLNSQYGYQIVAPFVTATQAQDTNYTLSTISM
STTPSTVTVPTWSFPGACAFQVQEGRVVVQIGDYAATELGSGDVAFIPGG
VEFKYYSEAYFSKVLFVSSGSDGLDQNLVNGGEEWSSVSFPADW
3D structure
PDB1h1m Anaerobic Enzyme.Substrate Structures Provide Insight Into the Reaction Mechanism of the Copper- Dependent Quercetin 2,3-Dioxygenase.
ChainA
Resolution1.9 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 KMP A M51 V63 H66 H68 E73 F75 M123 L135 F136 P164 V177 M49 V61 H64 H66 E71 F73 M121 L133 F134 P158 V171
BS02 CU A 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:1h1m, PDBe:1h1m, PDBj:1h1m
PDBsum1h1m
PubMed12486225
UniProtQ7SIC2|QDOI_ASPJA Quercetin 2,3-dioxygenase

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