› 1g9q

X-ray diffraction
2.3Å resolution

COMPLEX STRUCTURE OF THE ADPR-ASE AND ITS SUBSTRATE ADP-RIBOSE

Released:
DOI: 10.2210/pdb1g9q/pdb
PDB entry 1g9q coloured by chain, front view.
PDB entry 1g9q coloured by chain, side view.
PDB entry 1g9q coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The structure of ADP-ribose pyrophosphatase reveals the structural basis for the versatility of the Nudix family.
Gabelli SB, Bianchet MA, Bessman MJ, Amzel LM
Nat Struct Biol 8 467-72 (2001)
PMID: 11323725

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

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188087 (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

1 bound ligand:
Ligand APR 2 x APR
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
0.195 0.195 0.255
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Structures and mechanisms of Nudix hydrolases.
Mildvan et al. (2005)
3 more

3 mentions without citation

Crystal structure and functional analysis of Dcp2p from Schizosaccharomyces pombe.
She et al. (2006)
2 more