Structure of PDB 3p9o Chain A Binding Site BS01
Receptor Information
>3p9o Chain A (length=295) Species:
5059
(Aspergillus flavus) [
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SAVKAARYGKDNVRVYKVHKDEKTGVQTVYEMTVCVLLEGEIETSYTKAD
NSVIVATDSIKNTIYITAKQNPVTPPELFGSILGTHFIEKYNHIHAAHVN
IVCHRWTRMDIDGKPHPHSFIRDSEEKRNVQVDVVEGKGIDIKSSLSGLT
VLKSTNSQFWGFLRDEYTTLKETWDRILSTDVDATWQWKNFSGLQEVRSH
VPKFDATWATAREVTLKTFAEDNSASVQATMYKMAEQILARQQLIETVEY
SLPNKHYFEIDLSWHKGLQNTGKNAEVFAPQSDPNGLIKCTVGRS
Ligand information
Ligand ID
AZI
InChI
InChI=1S/N3/c1-3-2/q-1
InChIKey
IVRMZWNICZWHMI-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0
[N-]=[N+]=[N-]
Formula
N3
Name
AZIDE ION
ChEMBL
CHEMBL79455
DrugBank
ZINC
PDB chain
3p9o Chain A Residue 302 [
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Receptor-Ligand Complex Structure
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PDB
3p9o
Structural analysis of urate oxidase in complex with its natural substrate inhibited by cyanide: mechanistic implications.
Resolution
1.45 Å
Binding residue
(original residue number in PDB)
F159 Q228
Binding residue
(residue number reindexed from 1)
F159 Q228
Annotation score
1
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
PDBsum
3p9o
PubMed
UniProt
Q00511
|URIC_ASPFL Uricase (Gene Name=uaZ)
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