› 1kvk

X-ray diffraction
2.4Å resolution

The Structure of Binary complex between a Mammalian Mevalonate Kinase and ATP: Insights into the Reaction Mechanism and Human Inherited Disease

Released:
DOI: 10.2210/pdb1kvk/pdb
PDB entry 1kvk coloured by chain, front view.
PDB entry 1kvk coloured by chain, side view.
PDB entry 1kvk coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
The structure of a binary complex between a mammalian mevalonate kinase and ATP: insights into the reaction mechanism and human inherited disease.
Fu Z, Wang M, Potter D, Miziorko HM, Kim JJ
J Biol Chem 277 18134-42 (2002)
PMID: 11877411

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147906 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mevalonate kinase Chain: A
Molecule details ›
Chain: A
Length: 395 amino acids
Theoretical weight: 42.03 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P17256 (Residues: 1-395; Coverage: 100%)
Gene name: Mvk
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand ATP 1 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21212
Unit cell:
a: 78.63Å b: 118.7Å c: 42.84Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.217 0.266
Expression system: Escherichia coli

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Citations

5 review citations

Structure and function of enzymes of the Leloir pathway for galactose metabolism.
Holden et al. (2003)
4 more

15 mentions without citation

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