Structure of PDB 5lhv Chain D

Receptor sequence

>5lhvD (length=248) Species: 666 (Vibrio cholerae)

KTVFHLGVTEADLNGATLAIIPGDPARVQKIAELMDNPVFLASHREYTVY
RAELDGQSVVVCSTGIGGPSTSIAVEELAQLGVRTFLRVGTTGAIQPHVN
VGDMIVTTGSVRLDGASLHFAPMEFPAVPDFDVATAMKAAAQESGATVHM
GVTASSDTFYPGQERYDTFTGRVVRRFQGSMKEWQDMGVLNFEMESATLL
TMCASSGLKAGCVAGVIINRTQPDHATLKETEARSIKVVVEAARKMLK

3D structure

• PDB: 5lhv X-ray structure of uridine phosphorylase from Vibrio cholerae in complex with uridine and sulfate ion at 1.29 A resolution
• Chain: D
• Resolution: 1.288 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): H5 G23 R27 R45 E77 R88 T91 R165 I217 I218 R220 L228
• 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	URI	D	T93 T94 G95 F161 Q165 E195 M196 E197	T91 T92 G93 F159 Q163 E193 M194 E195
BS02	URA	D	T94 G95 F161 Q165 R167 I220	T92 G93 F159 Q163 R165 I218

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:5lhv, PDBe:5lhv, PDBj:5lhv
• PDBsum: 5lhv
• UniProt: Q9K4U1