6asv

X-ray diffraction
2.21Å resolution

E. coli PRPP Synthetase

Released:

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:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribose-phosphate pyrophosphokinase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 335 amino acids
Theoretical weight: 36.43 KDa
Source organism: Escherichia coli O157:H7
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A719 (Residues: 1-315; Coverage: 100%)
Gene names: ECs1712, Z1978, prs, prsA
Sequence domains:
Structure domains: Rossmann fold

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: C2221
Unit cell:
a: 104.757Å b: 138.436Å c: 137.438Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.177 0.212
Expression system: Escherichia coli