Structure of PDB 1tgv Chain B

Receptor sequence
>1tgvB (length=242) Species: 562 (Escherichia coli) [Search protein sequence]
SDVFHLGLTKNDLQGATLAIVPGDPDRVEKIAALMDKPVKLASHREFTTW
RAELDGKPVIVCSTGIGGPSTSIAVEELAQLGIRTFLRIGTTGAIQPHIN
VGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHV
GVTASSDTFYPGQERYDTYSGRVVRHFKGSMEEWQAMGVMNYEMESATLL
TMCASQGLRAGMVAGVIVNRTQMKQTESHAVKIVVEAARRLL
3D structure
PDB1tgv Structures of E. coli Uridine Phosphorylase
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H8 G26 R30 R48 E80 R91 T94 R168 I220 V221 R223 M234
Catalytic site (residue number reindexed from 1) H5 G23 R27 R45 E77 R88 T91 R165 I217 V218 R220 M223
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 5UD B T94 T95 G96 F162 Q166 E196 M197 E198 I220 T91 T92 G93 F159 Q163 E193 M194 E195 I217
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004850 uridine phosphorylase activity
GO:0005524 ATP binding
GO:0016757 glycosyltransferase activity
GO:0016763 pentosyltransferase activity
GO:0030955 potassium ion binding
GO:0042802 identical protein binding
GO:0047847 deoxyuridine phosphorylase activity
Biological Process
GO:0006218 uridine catabolic process
GO:0006974 DNA damage response
GO:0009116 nucleoside metabolic process
GO:0009164 nucleoside catabolic process
GO:0009166 nucleotide catabolic process
GO:0044206 UMP salvage
GO:0046050 UMP catabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0032991 protein-containing complex

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Cellular Component
External links
PDB RCSB:1tgv, PDBe:1tgv, PDBj:1tgv
PDBsum1tgv
PubMed
UniProtP12758|UDP_ECOLI Uridine phosphorylase (Gene Name=udp)

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