Structure of PDB 5yja Chain B

Receptor sequence
>5yjaB (length=302) Species: 36824 (Bacillus sp. TB-90) [Search protein sequence]
MYYGKGDVFAYRTYLKPLTGVRTIPESPFSGRDHILFGVNVKISVGGTKL
LTSFTKGDNSLVVATDSMKNFIQKHLASYTGTTIEGFLEYVATSFLKKYS
HIEKISLIGEEIPFETTFAVKNGNRAASELVFKKSRNEYATAYLNMVRNE
DNTLNITEQQSGLAGLQLIKVSGNSFVGFIRDEYTTLPEDSNRPLFVYLN
IKWKYKNTEDSFGTNPENYVAAEQIRDIATSVFHETETLSIQHLIYLIGR
RILERFPQLQEVYFESQNHTWDKIVEEIEGKVYTEPRPPYGFQCFTVTQE
DL
3D structure
PDB5yja Hyperstabilization of Tetrameric Bacillus sp. TB-90 Urate Oxidase by Introducing Disulfide Bonds through Structural Plasticity.
ChainB
Resolution1.65 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) K5 T65 R193 Q242 T270
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 B Y11 A72 T73 Y3 A64 T65
BS02 AZA B F184 R201 S248 I249 Q250 F176 R193 S240 I241 Q242
BS03 OXY B N276 G302 N268 G291
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:5yja, PDBe:5yja, PDBj:5yja
PDBsum5yja
PubMed
UniProtQ45697|PUCL_BACSB Uric acid degradation bifunctional protein (Gene Name=uao)

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