Structure of PDB 3pkg Chain A Binding Site BS02
Receptor Information
>3pkg Chain A (length=295) Species:
5059
(Aspergillus flavus) [
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SAVKAARYGKDNVRVYKVHKDEKTGVQTVYEMTVCVLLEGEIETSYTKAD
NSVIVATDSIKNTIYITAKQNPVTPPELFGSILGTHFIEKYNHIHAAHVN
IVCHRWTRMDIDGKPHPHSFIRDSEEKRNVQVDVVEGKGIDIKSSLSGLT
VLKSTNSQFWGFLRDEYTTLKETWDRILSTDVDATWQWKNFSGLQEVRSH
VPKFDATWATAREVTLKTFAEDNSASVQATMYKMAEQILARQQLIETVEY
SLPNKHYFEIDLSWHKGLQNTGKNAEVFAPQSDPNGLIKCTVGRS
Ligand information
Ligand ID
XE
InChI
InChI=1S/Xe
InChIKey
FHNFHKCVQCLJFQ-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0
[Xe]
Formula
Xe
Name
XENON
ChEMBL
CHEMBL1236802
DrugBank
DB13453
ZINC
PDB chain
3pkg Chain A Residue 801 [
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Receptor-Ligand Complex Structure
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PDB
3pkg
Pressure-response analysis of anesthetic gases xenon and nitrous oxide on urate oxidase: a crystallographic study.
Resolution
1.602 Å
Binding residue
(original residue number in PDB)
F219 T230
Binding residue
(residue number reindexed from 1)
F219 T230
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:3pkg
,
PDBe:3pkg
,
PDBj:3pkg
PDBsum
3pkg
PubMed
21421845
UniProt
Q00511
|URIC_ASPFL Uricase (Gene Name=uaZ)
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