Structure of PDB 2icq Chain A Binding Site BS03
Receptor Information
>2icq Chain A (length=295) Species:
5059
(Aspergillus flavus) [
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SAVKAARYGKDNVRVYKVHKDEKTGVQTVYEMTVCVLLEGEIETSYTKAD
NSVIVATDSIKNTIYITAKQNPVTPPELFGSILGTHFIEKYNHIHAAHVN
IVCHRWTRMDIDGKPHPHSFIRDSEEKRNVQVDVVEGKGIDIKSSLSGLT
VLKSTNSQFWGFLRDEYTTLKETWDRILSTDVDATWQWKNFSGLQEVRSH
VPKFDATWATAREVTLKTFAEDNSASVQATMYKMAEQILARQQLIETVEY
SLPNKHYFEIDLSWHKGLQNTGKNAEVFAPQSDPNGLIKCTVGRS
Ligand information
Ligand ID
N2O
InChI
InChI=1S/N2O/c1-2-3
InChIKey
GQPLMRYTRLFLPF-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
CACTVS 3.341
[O-][N+]#N
OpenEye OEToolkits 1.5.0
N#[N+][O-]
Formula
N2 O
Name
NITROUS OXIDE;
NITROGEN OXIDE
ChEMBL
CHEMBL1234579
DrugBank
DB06690
ZINC
PDB chain
2icq Chain A Residue 601 [
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Receptor-Ligand Complex Structure
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PDB
2icq
Protein Crystallography under Xenon and Nitrous Oxide Pressure: Comparison with In Vivo Pharmacology Studies and Implications for the Mechanism of Inhaled Anesthetic Action
Resolution
1.75 Å
Binding residue
(original residue number in PDB)
V182 T215 F219 M234
Binding residue
(residue number reindexed from 1)
V182 T215 F219 M234
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:2icq
,
PDBe:2icq
,
PDBj:2icq
PDBsum
2icq
PubMed
17028130
UniProt
Q00511
|URIC_ASPFL Uricase (Gene Name=uaZ)
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