Structure of PDB 5efo Chain C Binding Site BS02
Receptor Information
>5efo Chain C (length=251) Species:
666
(Vibrio cholerae) [
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KTVFHLGVTEADLNGATLAIIPGDPARVQKIAELMDNPVFLASHREYTVY
RAELDGQSVVVCSTGIGGPSTSIAVEELAQLGVRTFLRVGTTGAIQPHVN
VGDMIVTTGSVRLDGASLHFAPMEFPAVPDFDVATAMKAAAQESGATVHM
GVTASSDTFYPGQERYDTFTGRVVRRFQGSMKEWQDMGVLNFEMESATLL
TMCASSGLKAGCVAGVIINRTQKEIPDHATLKETEARSIKVVVEAARKML
K
Ligand information
Ligand ID
CYT
InChI
InChI=1S/C4H5N3O/c5-3-1-2-6-4(8)7-3/h1-2H,(H3,5,6,7,8)
InChIKey
OPTASPLRGRRNAP-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
O=C1N=CC=C(N)N1
OpenEye OEToolkits 1.5.0
C1=C(NC(=O)N=C1)N
CACTVS 3.341
NC1=CC=NC(=O)N1
Formula
C4 H5 N3 O
Name
6-AMINOPYRIMIDIN-2(1H)-ONE;
CYTOSINE
ChEMBL
CHEMBL15913
DrugBank
ZINC
ZINC000000895210
PDB chain
5efo Chain C Residue 304 [
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Receptor-Ligand Complex Structure
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PDB
5efo
X-ray structure uridine phosphorylase from Vibrio cholerae in complex with uridine at 2.24 A resolution
Resolution
1.63 Å
Binding residue
(original residue number in PDB)
R178 F179 W186
Binding residue
(residue number reindexed from 1)
R176 F177 W184
Annotation score
1
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 L231
Enzyme Commision number
2.4.2.3
: uridine phosphorylase.
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
PDBsum
5efo
PubMed
UniProt
Q9K4U1
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