› 2r3v

X-ray diffraction
2.5Å resolution

The Biochemical and Structural Basis for Feedback Inhibition of Mevalonate Kinase and Isoprenoid Metabolism

Released:
DOI: 10.2210/pdb2r3v/pdb
PDB entry 2r3v coloured by chain, front view.
PDB entry 2r3v coloured by chain, side view.
PDB entry 2r3v coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Biochemical and structural basis for feedback inhibition of mevalonate kinase and isoprenoid metabolism.
Fu Z, Voynova NE, Herdendorf TJ, Miziorko HM, Kim JJ
Biochemistry 47 3715-24 (2008)
PMID: 18302342

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-169887 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mevalonate kinase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 396 amino acids
Theoretical weight: 42.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q03426 (Residues: 1-396; Coverage: 100%)
Gene name: MVK
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 102.03Å b: 78.2Å c: 109.45Å
α: 90° β: 113.33° γ: 90°
R-values:
R R work R free
0.239 0.239 0.282
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Enzymes of the mevalonate pathway of isoprenoid biosynthesis.
Miziorko HM. (2011)
3 more

3 mentions without citation

The structure and dynamics of BmR1 protein from Brugia malayi: in silico approaches.
Khor et al. (2014)
2 more