Structure of PDB 2yze Chain A Binding Site BS02

Receptor Information
>2yze Chain A (length=287) Species: 1665 (Arthrobacter globiformis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TKVVLGQNQYGKAEVRLVKVTRNTARHEIQDLNVTSQLRGDFEAAHTAGD
NAHVVATDTQKNTVYAFARDGFATTEEFLLRLGKHFTEGFDWVTGGRWAA
QQFFWDRINDHDHAFSRNKSEVRTAVLEISGSEQAIVAGIEGLTVLKSTG
SEFHGFPRDKYTTLQETTDRILATDVSARWRYNTVEVDFDAVYASVRGLL
LKAFAETHSLALQQTMYEMGRAVIETHPEIDEIKMSLPNKHHFLVDLQPF
GQDNPNEVFYAADRPYGLIEATIQREGSRADHPIWSN
Ligand information
Ligand IDNOB
InChIInChI=1S/B2H3O5.Li/c3-1(4)7-2(5)6;/h3-5H;/q-1;+1
InChIKeyOBDSFKZXLCSJJG-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[Li]OB(O)OB(O)O
FormulaB2 H3 Li O5
Name(dihydroxyboranyloxy-hydroxy-boranyl)oxylithium
ChEMBL
DrugBank
ZINC
PDB chain2yze Chain D Residue 404 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2yze Trapping of the uric acid substrate in the crystal structure of urate oxidase from Arthrobacter globiformis
Resolution1.99 Å
Binding residue
(original residue number in PDB)		A66 T67
Binding residue
(residue number reindexed from 1)		A56 T57
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K22 T67 R180 Q223 H251
Catalytic site (residue number reindexed from 1) K12 T57 R170 Q213 H241
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:0019628 urate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2yze, PDBe:2yze, PDBj:2yze
PDBsum2yze
PubMed
UniProtD0VWQ1|URIC_ARTGO Uricase (Gene Name=uox)

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