Structure of PDB 4r2x Chain D

Receptor sequence
>4r2xD (length=249) Species: 211586 (Shewanella oneidensis MR-1) [Search protein sequence]
ADVFHLGLTKAMLDGATLAIVPGDPERVKRIAELMDNATFLASHREYTSY
LAYADGKPVVICSTGIGGPSTSIAVEELAQLGVNTFLRVGTTGAIQPHVN
VGDVIVTQASVRLDGASLHFAPMEFPAVANFECTTAMVAACRDAGVEPHI
GVTASSDTFYPGQERYDTVTGRVTRRFAGSMKEWQDMGVLNYEMESATLF
TMCATQGWRAACVAGVIVNRTQQEIPDEATMKEVSAVSIVVAAAKKLLA
3D structure
PDB4r2x High-syn conformation of uridine and asymmetry of the hexameric molecule revealed in the high-resolution structures of Shewanella oneidensis MR-1 uridine phosphorylase in the free form and in complex with uridine.
ChainD
Resolution0.93 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H5 G23 R27 R45 E77 R88 T91 R165 I217 V218 R220 M231
Catalytic site (residue number reindexed from 1) H5 G23 R27 R45 E77 R88 T91 R165 I217 V218 R220 M231
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 SO4 D G23 R27 R88 G90 T91 G23 R27 R88 G90 T91
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:4r2x, PDBe:4r2x, PDBj:4r2x
PDBsum4r2x
PubMed25478848
UniProtQ8E9X9

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