3kh5

X-ray diffraction
2.1Å resolution

Crystal Structure of Protein MJ1225 from Methanocaldococcus jannaschii, a putative archaeal homolog of g-AMPK.

Released:

Function and Biology Details

Reaction catalysed:
(R)-mevalonate + CoA + 2 NADP(+) = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
protein MJ1225 Chain: A
Molecule details ›
Chain: A
Length: 280 amino acids
Theoretical weight: 31.76 KDa
Source organism: Methanocaldococcus jannaschii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q58622 (Residues: 1-280; Coverage: 100%)
Gene name: MJ1225
Sequence domains: CBS domain
Structure domains: CBS-domain

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: R32
Unit cell:
a: 108.548Å b: 108.548Å c: 143.627Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.231 0.228 0.294
Expression system: Escherichia coli