X-ray diffraction
2.3Å resolution

Structure of malonyl-coenzyme A reductase from crenarchaeota in complex with CoA

Entry authors: Demmer U, Warkentin E, Srivastava A, Kockelkorn D, Fuchs G, Ermler U

Function and Biology Details

Reaction catalysed:
Malonate semialdehyde + CoA + NADP(+) = malonyl-CoA + NADPH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Malonyl-CoA reductase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 359 amino acids
Theoretical weight: 39.61 KDa
Source organism: Sulfurisphaera tokodaii str. 7
Expression system: Escherichia coli
  • Canonical: Q96YK1 (Residues: 1-359; Coverage: 100%)
Gene names: STK_21710, mcr, scr
Sequence domains:
Structure domains:

Ligands and Environments

Cofactor: Ligand COA 6 x COA
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: C2221
Unit cell:
a: 111.63Å b: 137.62Å c: 362.01Å
α: 90° β: 90° γ: 90°
R R work R free
0.201 0.198 0.247
Expression system: Escherichia coli