Structure of PDB 4yjk Chain F

Receptor sequence

>4yjkF (length=244) Species: 211586 (Shewanella oneidensis MR-1)

ADVFHLGLTKAMLDGATLAIVPGDPERVKRIAELMDNATFLASHREYTSY
LAYADGKPVVICSTGIGGPSTSIAVEELAQLGVNTFLRVGTTGAIQPHVN
VGDVIVTQASVRLDGASLHFAPMEFPAVANFECTTAMVAACRDAGVEPHI
GVTASSDTFYPGQERYDTVTGRVTRRFAGSMKEWQDMGVLNYEMESATLF
TMCATQGWRAASVAGVIVNRTQQEIPDEVSAVSIVVAAAKKLLA

3D structure

• PDB: 4yjk Concerted action of two subunits of the functional dimer of Shewanella oneidensis MR-1 uridine phosphorylase derived from a comparison of the C212S mutant and the wild-type enzyme.
• Chain: F
• Resolution: 1.68 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H5 G23 R27 R45 E77 R88 T91 R165 I217 V218 R220
• Catalytic site (residue number reindexed from 1): H5 G23 R27 R45 E77 R88 T91 R165 I217 V218 R220
• 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	URA	F	T92 G93 F159 Q163 R165 Y192 E193	T92 G93 F159 Q163 R165 Y192 E193

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

External links

• PDB: RCSB:4yjk, PDBe:4yjk, PDBj:4yjk
• PDBsum: 4yjk
• PubMed: 26894668
• UniProt: Q8E9X9