Structure of PDB 2rj3 Chain B

Receptor sequence
>2rj3B (length=250) [Search protein sequence]
SDVFHLGLTKNDLQGAQLAIVPGDPERVEKIAALMDKPVKLASHREFTSW
RAELDGKAVIVCSTGIGGPSTSIAVEELAQLGIRTFLRIGTTGAIQPHIN
VGDVLVTTASVRLDGASLHFAPMEFPAVADFACTTALVEAAKSIGATTHV
GVTASSDTFYPGQERYDTYSGRVVRRFKGSMEEWQAMGVMNYEMESATLL
TMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVKIVVEAARRLL
3D structure
PDB2rj3 Crystal Structure of the Uridine Phosphorylase from Salmonella Typhimurium in Complex with Uracil and Phosphate Ion at 2.49A Resolution
ChainB
Resolution2.51 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H6008 G6026 R6030 R6048 E6080 R6091 T6094 R6168 I6220 V6221 R6223 M6234
Catalytic site (residue number reindexed from 1) H5 G23 R27 R45 E77 R88 T91 R165 I217 V218 R220 M231
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 URA B T6094 T6095 G6096 F6162 Q6166 R6168 I6220 T91 T92 G93 F159 Q163 R165 I217
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
GO:0005829 cytosol

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Molecular Function

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Cellular Component
External links
PDB RCSB:2rj3, PDBe:2rj3, PDBj:2rj3
PDBsum2rj3
PubMed
UniProtP0A1F6|UDP_SALTY Uridine phosphorylase (Gene Name=udp)

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