› 2v34

X-ray diffraction
2.3Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol = ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130425 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-diphosphocytidyl-2-C-methyl-D-erythritol kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 271 amino acids
Theoretical weight: 30.1 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O67060 (Residues: 1-268; Coverage: 100%)
Gene names: aq_915, ispE
Sequence domains: GHMP kinases N terminal domain
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand CTN 2 x CTN
Ligand CL 2 x CL
Ligand SO4 8 x SO4
Ligand SG3 1 x SG3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P213
Unit cell:
a: 137.169Å b: 137.169Å c: 137.169Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.197 0.245
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

Molecular recognition in chemical and biological systems.
Persch et al. (2015)
6 more