Structure of PDB 1h1m Chain D Binding Site BS01

Receptor Information
>1h1m Chain D (length=343) Species: 34381 (Aspergillus japonicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SLIVEDAPDHVRPYVIRHYSHARAVTVDTQLYRFYVTGPSSGYAFTLMGT
NAPHSDALGVLPHIHQKHYENFYCNKGSFQLWAQSGNETQQTRVLSSGDY
GSVPRNVTHTFQIQDPDTEMTGVIVPGGFEDLFYYLGTNATDTTHTPYIP
SSSTTGPDSSTISTLQSFDVYAELSFTPRTDTVNGTAPANTVWHTGANAL
ASTAGDPYFIANGWGPKYLNSQYGYQIVAPFVTATQAQDTNYTLSTISMS
TTPSTVTVPTWSFPGACAFQVQEGRVVVQIGDYAATELGSGDVAFIPGGV
EFKYYSEAYFSKVLFVSSGSDGLDQNLVNGGEEWSSVSFPADW
Ligand information
Ligand IDKMP
InChIInChI=1S/C15H10O6/c16-8-3-1-7(2-4-8)15-14(20)13(19)12-10(18)5-9(17)6-11(12)21-15/h1-6,16-18,20H
InChIKeyIYRMWMYZSQPJKC-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1cc(ccc1C2=C(C(=O)c3c(cc(cc3O2)O)O)O)O
CACTVS 3.341Oc1ccc(cc1)C2=C(O)C(=O)c3c(O)cc(O)cc3O2
ACDLabs 10.04O=C1c3c(OC(=C1O)c2ccc(O)cc2)cc(O)cc3O
FormulaC15 H10 O6
Name3,5,7-TRIHYDROXY-2-(4-HYDROXYPHENYL)-4H-CHROMEN-4-ONE;
KAEMPHEROL
ChEMBLCHEMBL150
DrugBankDB01852
ZINCZINC000003869768
PDB chain1h1m Chain D Residue 1356 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1h1m Anaerobic Enzyme.Substrate Structures Provide Insight Into the Reaction Mechanism of the Copper- Dependent Quercetin 2,3-Dioxygenase.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		Y35 M51 V63 H66 H68 E73 F75 F114 L135 F136 P164 V177
Binding residue
(residue number reindexed from 1)		Y32 M48 V60 H63 H65 E70 F72 F111 L132 F133 P157 V170
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) H66 H68 E73 H112
Catalytic site (residue number reindexed from 1) H63 H65 E70 H109
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

View graph for
Molecular Function
External links
PDB RCSB:1h1m, PDBe:1h1m, PDBj:1h1m
PDBsum1h1m
PubMed12486225
UniProtQ7SIC2|QDOI_ASPJA Quercetin 2,3-dioxygenase

[Back to BioLiP]