› 3dah

X-ray diffraction
2.3Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo trimer (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-179099 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribose-phosphate pyrophosphokinase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 319 amino acids
Theoretical weight: 34.34 KDa
Source organism: Burkholderia pseudomallei 1710b
Expression system: Escherichia coli
UniProt:
  • Canonical: Q63XL8 (Residues: 1-318; Coverage: 100%)
Gene names: BPSL0521, prs
Sequence domains:
Structure domains: Rossmann fold

Ligands and Environments

2 bound ligands:
Ligand PO4 7 x PO4
Ligand AMP 3 x AMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: I222
Unit cell:
a: 77.966Å b: 123.242Å c: 197.364Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.206 0.255
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.
Dailey et al. (2017)
9 more

6 mentions without citation

Phosphoribosyl Diphosphate (PRPP): Biosynthesis, Enzymology, Utilization, and Metabolic Significance.
Hove-Jensen et al. (2017)
5 more