Structure of PDB 5yj2 Chain A Binding Site BS03
Receptor Information
>5yj2 Chain A (length=303) Species:
36824
(Bacillus sp. TB-90) [
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VMYYGKGDVFAYRTYLKPLTGVRTIPESPFSGRDHILFGVNVKISVGGTK
LLTSFTKGDNSLVVATDSMKNFIQKHLASYTGTTIEGFLEYVATSFLKKY
SHIEKISLIGEEIPFETTFAVKNGNRAASELVFKKSRNEYATAYLNMVRN
EDNTLNITEQQSGLAGLQLIKVSGNSFVGFIRDEYTTLPEDSNRPLFVYL
NIKWKYKNTEDSFGTNPENYVAAEQIRDIATSVFHETETLSIQHLIYLIG
RRILERFPQLQEVYFESQNHTWDKIVEEIPESEGKVYTEPRPPYGFQCFT
VTQ
Ligand information
Ligand ID
MXE
InChI
InChI=1S/C3H8O2/c1-5-3-2-4/h4H,2-3H2,1H3
InChIKey
XNWFRZJHXBZDAG-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
OpenEye OEToolkits 1.5.0
COCCO
ACDLabs 10.04
OCCOC
Formula
C3 H8 O2
Name
2-METHOXYETHANOL
ChEMBL
CHEMBL444144
DrugBank
DB02806
ZINC
ZINC000001591817
PDB chain
5yj2 Chain A Residue 403 [
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Receptor-Ligand Complex Structure
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PDB
5yj2
Hyperstabilization of Tetrameric Bacillus sp. TB-90 Urate Oxidase by Introducing Disulfide Bonds through Structural Plasticity.
Resolution
1.71 Å
Binding residue
(original residue number in PDB)
Q275 F303 C305
Binding residue
(residue number reindexed from 1)
Q268 F296 C298
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
K13 T73 R201 Q250 T278
Catalytic site (residue number reindexed from 1)
K6 T66 R194 Q243 T271
Enzyme Commision number
1.7.3.3
: factor independent urate hydroxylase.
4.1.1.97
: 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase.
Gene Ontology
Molecular Function
GO:0004846
urate oxidase activity
Biological Process
GO:0006144
purine nucleobase metabolic process
View graph for
Molecular Function
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Biological Process
External links
PDB
RCSB:5yj2
,
PDBe:5yj2
,
PDBj:5yj2
PDBsum
5yj2
PubMed
UniProt
Q45697
|PUCL_BACSB Uric acid degradation bifunctional protein (Gene Name=uao)
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