Structure of PDB 5yj2 Chain C

Receptor sequence
>5yj2C (length=303) Species: 36824 (Bacillus sp. TB-90) [Search protein sequence]
VMYYGKGDVFAYRTYLKPLTGVRTIPESPFSGRDHILFGVNVKISVGGTK
LLTSFTKGDNSLVVATDSMKNFIQKHLASYTGTTIEGFLEYVATSFLKKY
SHIEKISLIGEEIPFETTFAVKNGNRAASELVFKKSRNEYATAYLNMVRN
EDNTLNITEQQSGLAGLQLIKVSGNSFVGFIRDEYTTLPEDSNRPLFVYL
NIKWKYKNTEDSFGTNPENYVAAEQIRDIATSVFHETETLSIQHLIYLIG
RRILERFPQLQEVYFESQNHTWDKIVEEIPESEGKVYTEPRPPYGFQCFT
VTQ
3D structure
PDB5yj2 Hyperstabilization of Tetrameric Bacillus sp. TB-90 Urate Oxidase by Introducing Disulfide Bonds through Structural Plasticity.
ChainC
Resolution1.71 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 AZA C F184 R201 S248 I249 Q250 F177 R194 S241 I242 Q243
BS02 OXY C N276 G302 N269 G295
BS03 MXE C Y301 C305 Y294 C298
BS04 AZA C A72 T73 A65 T66
Gene Ontology
Molecular Function
GO:0004846 urate oxidase activity
Biological Process
GO:0006144 purine nucleobase metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5yj2, PDBe:5yj2, PDBj:5yj2
PDBsum5yj2
PubMed
UniProtQ45697|PUCL_BACSB Uric acid degradation bifunctional protein (Gene Name=uao)

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