› 1opr

X-ray diffraction
2.3Å resolution

THE CRYSTAL STRUCTURE OF THE OROTATE PHOSPHORIBOSYLTRANSFERASE COMPLEXED WITH OROTATE AND ALPHA-D-5-PHOSPHORIBOSYL-1-PYROPHOSPHATE

Released:
DOI: 10.2210/pdb1opr/pdb
PDB entry 1opr coloured by chain, front view.
PDB entry 1opr coloured by chain, side view.
PDB entry 1opr coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Primary publication:
The crystal structure of the orotate phosphoribosyltransferase complexed with orotate and alpha-D-5-phosphoribosyl-1-pyrophosphate.
Scapin G, Ozturk DH, Grubmeyer C, Sacchettini JC
Biochemistry 34 10744-54 (1995)
PMID: 7545004

Function and Biology Details

Reaction catalysed: 
Orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140401 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Orotate phosphoribosyltransferase Chain: A
Molecule details ›
Chain: A
Length: 213 amino acids
Theoretical weight: 23.59 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli
UniProt:
  • Canonical: P08870 (Residues: 1-213; Coverage: 100%)
Gene names: STM3733, pyrE
Sequence domains: Phosphoribosyl transferase domain
Structure domains: Rossmann fold

Ligands and Environments

3 bound ligands:
Ligand MG 1 x MG
Ligand ORO 1 x ORO
Ligand PRP 1 x PRP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P41212
Unit cell:
a: 47.3Å b: 47.3Å c: 216.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 not available
Expression system: Escherichia coli

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Citations

4 review citations

Enzymatic transition states and transition state analog design.
Schramm VL. (1998)
3 more

6 mentions without citation

Predicting protein function from structure: unique structural features of proteases.
Stawiski et al. (2000)
5 more