1g0s

X-ray diffraction
1.9Å resolution

THE CRYSTAL STRUCTURE OF THE E.COLI ADP-RIBOSE PYROPHOSPHATASE

Released:

Function and Biology Details

Reaction catalysed:
ADP-D-ribose + H(2)O = AMP + D-ribose 5-phosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ADP-ribose pyrophosphatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 209 amino acids
Theoretical weight: 23.7 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: Q93K97 (Residues: 1-209; Coverage: 100%)
Gene names: JW3002, aspP, b3034, nudF, yqiE, yzzG
Sequence domains: NUDIX domain
Structure domains: Nucleoside Triphosphate Pyrophosphohydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P212121
Unit cell:
a: 66.93Å b: 67.89Å c: 98.07Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.192 0.241
Expression system: Escherichia coli