Structure of PDB 3kvr Chain B

Receptor sequence
>3kvrB (length=293) Species: 9913 (Bos taurus) [Search protein sequence]
HNDLVQLCNPHIAAMKEDILYHFSLSTSTHDFPAMFGDVKFVCVGGSPSR
MKAFIKYVAMELGFAHDYPNICEGTDRYAMFKVGPVLSVSHGMGVPSIAI
MLHELIKLLYHAHCSGVTLIRIGTSGGIGLEPGSVVITRQAVDPCFKPEF
EQIVLGKREVRNTDLDEQLVQELARCSAELGEFPTVVGNTMCTLDFYEGQ
GRLDGALCSYTEKDKQDYLRAAYAAGIRNIEMEASVFAAMCNACGLRAAV
VCVTLLNRLEGDQISSPHDVLAEYQQRPQRLVGQFIKKRLMQA
3D structure
PDB3kvr Glycal formation in crystals of uridine phosphorylase.
ChainB
Resolution2.6 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) E104 R258
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 URF B T140 S141 G142 F212 Q216 R218 I246 L271 T124 S125 G126 F196 Q200 R202 I230 L255
BS02 SO4 B G59 R63 R137 T140 G46 R50 R121 T124
BS03 R2G B M109 T140 E249 M93 T124 E233
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:3kvr, PDBe:3kvr, PDBj:3kvr
PDBsum3kvr
PubMed20364833
UniProtA5PJH9

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