Structure of PDB 3p9o Chain A Binding Site BS02

Receptor Information
>3p9o Chain A (length=295) Species: 5059 (Aspergillus flavus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SAVKAARYGKDNVRVYKVHKDEKTGVQTVYEMTVCVLLEGEIETSYTKAD
NSVIVATDSIKNTIYITAKQNPVTPPELFGSILGTHFIEKYNHIHAAHVN
IVCHRWTRMDIDGKPHPHSFIRDSEEKRNVQVDVVEGKGIDIKSSLSGLT
VLKSTNSQFWGFLRDEYTTLKETWDRILSTDVDATWQWKNFSGLQEVRSH
VPKFDATWATAREVTLKTFAEDNSASVQATMYKMAEQILARQQLIETVEY
SLPNKHYFEIDLSWHKGLQNTGKNAEVFAPQSDPNGLIKCTVGRS
Ligand information
Ligand IDAZI
InChIInChI=1S/N3/c1-3-2/q-1
InChIKeyIVRMZWNICZWHMI-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[N-]=[N+]=[N-]
FormulaN3
NameAZIDE ION
ChEMBLCHEMBL79455
DrugBank
ZINC
PDB chain3p9o Chain A Residue 303 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3p9o Structural analysis of urate oxidase in complex with its natural substrate inhibited by cyanide: mechanistic implications.
Resolution1.45 Å
Binding residue
(original residue number in PDB)		A5 A6 R7
Binding residue
(residue number reindexed from 1)		A5 A6 R7
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K10 T57 R176 Q228 H256
Catalytic site (residue number reindexed from 1) K10 T57 R176 Q228 H256
Enzyme Commision number 1.7.3.3: factor independent urate hydroxylase.
Gene Ontology
Molecular Function
GO:0004846 urate oxidase activity
GO:0016491 oxidoreductase activity
Biological Process
GO:0006144 purine nucleobase metabolic process
GO:0006145 purine nucleobase catabolic process
GO:0019628 urate catabolic process
Cellular Component
GO:0005777 peroxisome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3p9o, PDBe:3p9o, PDBj:3p9o
PDBsum3p9o
PubMed
UniProtQ00511|URIC_ASPFL Uricase (Gene Name=uaZ)

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