4hac

X-ray diffraction
1.92Å resolution

Crystal Structure of the Mevalonate Kinase from an Archaeon Methanosarcina mazei

Released:
Source organism: Methanosarcina mazei Go1
Primary publication:
Crystallization and preliminary X-ray diffraction analysis of mevalonate kinase from Methanosarcina mazei.
Acta Crystallogr Sect F Struct Biol Cryst Commun 68 1560-3 (2012)
PMID: 23192048

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185812 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Mevalonate kinase Chain: A
Molecule details ›
Chain: A
Length: 321 amino acids
Theoretical weight: 33.8 KDa
Source organism: Methanosarcina mazei Go1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8PW39 (Residues: 1-301; Coverage: 100%)
Gene names: MM_1762, mvk
Sequence domains:
Structure domains:
Mevalonate kinase Chain: B
Molecule details ›
Chain: B
Length: 321 amino acids
Theoretical weight: 33.85 KDa
Source organism: Methanosarcina mazei Go1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8PW39 (Residues: 1-301; Coverage: 100%)
Gene names: MM_1762, mvk
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: OTHER
Spacegroup: P21212
Unit cell:
a: 97.295Å b: 135.359Å c: 45.867Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.211 0.263
Expression system: Escherichia coli BL21(DE3)