Structure of PDB 3kvy Chain A

Receptor sequence
>3kvyA (length=290) Species: 9913 (Bos taurus) [Search protein sequence]
DLVQLCNPHIAAMKEDILYHFSLSTSTHDFPAMFGDVKFVCVGGSPSRMK
AFIKYVAMELGFAADYPNICEGTDRYAMFKVGPVLSVSHGMGVPSIAIML
HELIKLLYHAHCSGVTLIRIGTSGGIGLEPGSVVITRQAVDPCFKPEFEQ
IVLGKREVRNTDLDEQLVQELARCSAELGEFPTVVGNTMCTLDFYEGQGR
LDGALCSYTEKDKQDYLRAAYAAGIRNIEMEASVFAAMCNACGLRAAVVC
VTLLNRLEGDQISSPHDVLAEYQQRPQRLVGQFIKKRLMQ
3D structure
PDB3kvy Glycal formation in crystals of uridine phosphorylase.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E120 R274
Catalytic site (residue number reindexed from 1) E102 R256
Enzyme Commision number 2.4.2.3: uridine phosphorylase.
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 SO4 A G59 R137 T140 G44 R119 T122
BS02 URA A S141 G142 F212 Q216 R218 I246 E247 M248 S123 G124 F194 Q198 R200 I228 E229 M230
BS03 R2B A M109 T140 M248 E249 M91 T122 M230 E231
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004850 uridine phosphorylase activity
GO:0016757 glycosyltransferase activity
GO:0016763 pentosyltransferase activity
GO:0047847 deoxyuridine phosphorylase activity
Biological Process
GO:0009116 nucleoside metabolic process
GO:0009164 nucleoside catabolic process
GO:0009166 nucleotide catabolic process
GO:0044206 UMP salvage
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3kvy, PDBe:3kvy, PDBj:3kvy
PDBsum3kvy
PubMed20364833
UniProtA5PJH9

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