Structure of PDB 3fwp Chain D Binding Site BS01
Receptor Information
>3fwp Chain D (length=241) [
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SDVFHLGLTKNDLQGAQLAIVPGDPERVEKIAALMDKPVKLASHREFTSW
RAELDGKAVIVCSTGIGGPSTSIAVEELAQLGIRTFLRIGTTGAIQPHIN
VGDVLVTTASVRLDGASLHFAPMEFPAVADFACTTALVEAAKSIGATTHV
GVTASSDTFYPGQERYDTYSGRVVRRFKGSMEEWQAMGVMNYEMESATLL
TMCASQGLRAGMVAGVIVNRTMKQTESHAVKIVVEAARRLL
Ligand information
Ligand ID
K
InChI
InChI=1S/K/q+1
InChIKey
NPYPAHLBTDXSSS-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0
[K+]
Formula
K
Name
POTASSIUM ION
ChEMBL
CHEMBL1233793
DrugBank
DB01345
ZINC
PDB chain
3fwp Chain B Residue 8001 [
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Receptor-Ligand Complex Structure
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PDB
3fwp
The X-ray structure of Salmonella typhimurium uridine nucleoside phosphorylase complexed with 2,2'-anhydrouridine, phosphate and potassium ions at 1.86 A resolution.
Resolution
1.86 Å
Binding residue
(original residue number in PDB)
E3049 G3068 I3069 S3073
Binding residue
(residue number reindexed from 1)
E46 G65 I66 S70
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
R3030 R3048 R3091 R3168 I3220 V3221
Catalytic site (residue number reindexed from 1)
R27 R45 R88 R165 I217 V218
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: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:3fwp
,
PDBe:3fwp
,
PDBj:3fwp
PDBsum
3fwp
PubMed
20057049
UniProt
P0A1F6
|UDP_SALTY Uridine phosphorylase (Gene Name=udp)
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