Structure of PDB 5lok Chain B

Receptor sequence

>5lokB (length=252) Species: 666 (Vibrio cholerae)

TKTVFHLGVTEADLNGATLAIIPGDPARVQKIAELMDNPVFLASHREYTV
YRAELDGQSVVVCSTGIGGPSTSIAVEELAQLGVRTFLRVGTTGAIQPHV
NVGDMIVTTGSVRLDGASLHFAPMEFPAVPDFDVATAMKAAAQESGATVH
MGVTASSDTFYPGQERYDTFTGRVVRRFQGSMKEWQDMGVLNFEMESATL
LTMCASSGLKAGCVAGVIINRTQKEIPDHATLKETEARSIKVVVEAARKM
LK

3D structure

• PDB: 5lok X-ray structure of uridine phosphorylase from Vibrio cholerae in complex with cytidine and cytosine at 1.11 A resolution
• Chain: B
• Resolution: 1.109 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H7 G25 R29 R47 E79 R90 T93 R167 I219 I220 R222 L233
• Catalytic site (residue number reindexed from 1): H6 G24 R28 R46 E78 R89 T92 R166 I218 I219 R221 L232
• 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	CTN	B	T93 T94 G95 F161 Q165 E195 M196 E197 I220	T92 T93 G94 F160 Q164 E194 M195 E196 I219
BS02	CYT	B	T94 G95 F161 Q165 I220	T93 G94 F160 Q164 I219

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0004850 uridine phosphorylase activity
• GO:0016757 glycosyltransferase activity
• GO:0016763 pentosyltransferase activity
• GO:0046872 metal ion binding
• 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

External links

• PDB: RCSB:5lok, PDBe:5lok, PDBj:5lok
• PDBsum: 5lok
• UniProt: Q9K4U1