Structure of PDB 5lhv Chain B Binding Site BS02
Receptor Information
>5lhv Chain B (length=251) Species:
666
(Vibrio cholerae) [
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KTVFHLGVTEADLNGATLAIIPGDPARVQKIAELMDNPVFLASHREYTVY
RAELDGQSVVVCSTGIGGPSTSIAVEELAQLGVRTFLRVGTTGAIQPHVN
VGDMIVTTGSVRLDGASLHFAPMEFPAVPDFDVATAMKAAAQESGATVHM
GVTASSDTFYPGQERYDTFTGRVVRRFQGSMKEWQDMGVLNFEMESATLL
TMCASSGLKAGCVAGVIINRTQKEIPDHATLKETEARSIKVVVEAARKML
K
Ligand information
Ligand ID
URA
InChI
InChI=1S/C4H4N2O2/c7-3-1-2-5-4(8)6-3/h1-2H,(H2,5,6,7,8)
InChIKey
ISAKRJDGNUQOIC-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
O=C1NC=CC(=O)N1
ACDLabs 10.04
O=C1C=CNC(=O)N1
OpenEye OEToolkits 1.5.0
C1=CNC(=O)NC1=O
Formula
C4 H4 N2 O2
Name
URACIL
ChEMBL
CHEMBL566
DrugBank
DB03419
ZINC
ZINC000000895045
PDB chain
5lhv Chain B Residue 304 [
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Receptor-Ligand Complex Structure
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PDB
5lhv
X-ray structure of uridine phosphorylase from Vibrio cholerae in complex with uridine and sulfate ion at 1.29 A resolution
Resolution
1.288 Å
Binding residue
(original residue number in PDB)
T94 G95 F161 Q165 R167 I219 I220
Binding residue
(residue number reindexed from 1)
T92 G93 F159 Q163 R165 I217 I218
Annotation score
5
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:5lhv
,
PDBe:5lhv
,
PDBj:5lhv
PDBsum
5lhv
PubMed
UniProt
Q9K4U1
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