Structure of PDB 5efo Chain B

Receptor sequence
>5efoB (length=253) Species: 666 (Vibrio cholerae) [Search protein sequence]
MTKTVFHLGVTEADLNGATLAIIPGDPARVQKIAELMDNPVFLASHREYT
VYRAELDGQSVVVCSTGIGGPSTSIAVEELAQLGVRTFLRVGTTGAIQPH
VNVGDMIVTTGSVRLDGASLHFAPMEFPAVPDFDVATAMKAAAQESGATV
HMGVTASSDTFYPGQERYDTFTGRVVRRFQGSMKEWQDMGVLNFEMESAT
LLTMCASSGLKAGCVAGVIINRTQKEIPDHATLKETEARSIKVVVEAARK
MLK
3D structure
PDB5efo X-ray structure uridine phosphorylase from Vibrio cholerae in complex with uridine at 2.24 A resolution
ChainB
Resolution1.63 Å
3D
structure
Catalytic site residues are labeled in the structure
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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) H7 G25 R29 R47 E79 R90 T93 R167 I219 I220 R222 L233
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 CYT B T94 G95 F161 Q165 T94 G95 F161 Q165
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5efo, PDBe:5efo, PDBj:5efo
PDBsum5efo
PubMed
UniProtQ9K4U1

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