Structure of PDB 1rxu Chain H

Receptor sequence

>1rxuH (length=250) Species: 562 (Escherichia coli)

SDVFHLGLTKNDLQGATLAIVPGDPDRVEKIAALMDKPVKLASHREFTTW
RAELDGKPVIVCSTGIGGPSTSIAVEELAQLGIRTFLRIGTTGAIQPHIN
VGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHV
GVTASSDTFYPGQERYDTYSGRVVRHFKGSMEEWQAMGVMNYEMESATLL
TMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVKIVVEAARRLL

3D structure

• PDB: 1rxu Crystal structures of escherichia coli uridine phosphorylase in two native and three complexed forms reveal basis of substrate specificity, induced conformational changes and influence of potassium
• Chain: H
• Resolution: 3.1 Å

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 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	K	H	E49 G68 I69 S73	E46 G65 I66 S70

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

External links

• PDB: RCSB:1rxu, PDBe:1rxu, PDBj:1rxu
• PDBsum: 1rxu
• PubMed: 15003451
• UniProt: P12758|UDP_ECOLI Uridine phosphorylase (Gene Name=udp)