› 1nqz

X-ray diffraction
1.7Å resolution

The structure of a CoA pyrophosphatase from D. Radiodurans complexed with a magnesium ion

Released:
DOI: 10.2210/pdb1nqz/pdb
PDB entry 1nqz coloured by chain, front view.
PDB entry 1nqz coloured by chain, side view.
PDB entry 1nqz coloured by chain, top view.
Source organism: Deinococcus radiodurans
Primary publication:
Structure of a coenzyme A pyrophosphatase from Deinococcus radiodurans: a member of the Nudix family.
Kang LW, Gabelli SB, Bianchet MA, Xu WL, Bessman MJ, Amzel LM
J Bacteriol 185 4110-8 (2003)
PMID: 12837785

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193292 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nudix hydrolase DR_1184 Chain: A
Molecule details ›
Chain: A
Length: 194 amino acids
Theoretical weight: 21.27 KDa
Source organism: Deinococcus radiodurans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9RV46 (Residues: 1-194; Coverage: 100%)
Gene name: DR_1184
Sequence domains: NUDIX domain
Structure domains: Nucleoside Triphosphate Pyrophosphohydrolase

Ligands and Environments

1 bound ligand:
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21212
Unit cell:
a: 40.618Å b: 94.066Å c: 43.664Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.216 0.258
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

6 mentions without citation

OptMAVEn--a new framework for the de novo design of antibody variable region models targeting specific antigen epitopes.
Li et al. (2014)
5 more