› 1viq

X-ray diffraction
2.4Å resolution

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ADP-ribose pyrophosphatase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 220 amino acids
Theoretical weight: 24.88 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: Q93K97 (Residues: 2-209; 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: APS BEAMLINE 32-ID
Spacegroup: P3221
Unit cell:
a: 98.176Å b: 98.176Å c: 155.942Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.244 0.244 0.314
Expression system: Escherichia coli

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Citations

22 review citations

Fe-S cluster biogenesis by the bacterial Suf pathway.
Blahut et al. (2020)
21 more