› 1vis

X-ray diffraction
2.69Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + (R)-mevalonate = ADP + (R)-5-phosphomevalonate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176626 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mevalonate kinase Chain: A
Molecule details ›
Chain: A
Length: 324 amino acids
Theoretical weight: 36.59 KDa
Source organism: Methanocaldococcus jannaschii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q58487 (Residues: 2-312; Coverage: 100%)
Gene names: MJ1087, mvk
Sequence domains:
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: P21
Unit cell:
a: 56.347Å b: 44.506Å c: 65.88Å
α: 90° β: 103.09° γ: 90°
R-values:
R R work R free
0.275 0.275 0.337
Expression system: Escherichia coli

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Citations

23 review citations

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

2 mentions without citation

A general and robust ray-casting-based algorithm for triangulating surfaces at the nanoscale.
Decherchi et al. (2013)
1 more