› 3q4i

X-ray diffraction
2.5Å resolution

Crystal structure of CDP-Chase in complex with Gd3+

Released:
DOI: 10.2210/pdb3q4i/pdb
PDB entry 3q4i coloured by chain, front view.
PDB entry 3q4i coloured by chain, side view.
PDB entry 3q4i coloured by chain, top view.
Source organism: Bacillus cereus ATCC 14579
Primary publication:
The Nudix hydrolase CDP-chase, a CDP-choline pyrophosphatase, is an asymmetric dimer with two distinct enzymatic activities.
Duong-Ly KC, Gabelli SB, Xu W, Dunn CA, Schoeffield AJ, Bessman MJ, Amzel LM
J Bacteriol 193 3175-85 (2011)
PMID: 21531795

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182500 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nudix hydrolase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 205 amino acids
Theoretical weight: 23.72 KDa
Source organism: Bacillus cereus ATCC 14579
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q81EE8 (Residues: 1-205; Coverage: 100%)
Gene name: BC_2032
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand GD3 3 x GD3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P212121
Unit cell:
a: 61.005Å b: 70.855Å c: 111.793Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.222 0.288
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Nucleotide Sugars in Chemistry and Biology.
Mikkola S. (2020)
7 other articles

1 mention without citation

The Nudix hydrolase CDP-chase, a CDP-choline pyrophosphatase, is an asymmetric dimer with two distinct enzymatic activities.
Duong-Ly et al. (2011)