› 1vha

X-ray diffraction
2.35Å resolution

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo trimer (preferred)
homo dodecamer
Assembly name:
PDBe Complex ID:
PDB-CPX-155213 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 170 amino acids
Theoretical weight: 18.76 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli
UniProt:
  • Canonical: P44815 (Residues: 2-158; Coverage: 99%)
Gene names: HI_0671, ispF
Sequence domains: YgbB family
Structure domains: 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase

Ligands and Environments

3 bound ligands:
Ligand MN 5 x MN
Ligand ACY 6 x ACY
Ligand POP 2 x POP
1 modified residue:
Ligand MSE 24 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: I41
Unit cell:
a: 104.715Å b: 104.715Å c: 195.864Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.244 0.244 0.288
Expression system: Escherichia coli

Quick links

Citations

23 review citations

Regulation of fatty acid metabolism in bacteria.
Fujita et al. (2007)
22 more

1 mention without citation

Secondary structure preferences of mn (2+) binding sites in bacterial proteins.
Khrustaleva TA. (2014)