› 4dpk

X-ray diffraction
2.05Å resolution

Structure of malonyl-coenzyme A reductase from crenarchaeota

Released:
DOI: 10.2210/pdb4dpk/pdb
PDB entry 4dpk coloured by chain, front view.
PDB entry 4dpk coloured by chain, side view.
PDB entry 4dpk coloured by chain, top view.
Source organism: Sulfurisphaera tokodaii str. 7
Primary publication:
Structural basis for a bispecific NADP+ and CoA binding site in an archaeal malonyl-coenzyme A reductase.
Demmer U, Warkentin E, Srivastava A, Kockelkorn D, Pötter M, Marx A, Fuchs G, Ermler U
J Biol Chem 288 6363-70 (2013)
PMID: 23325803

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188794 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Malonyl-CoA reductase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 359 amino acids
Theoretical weight: 39.61 KDa
Source organism: Sulfurisphaera tokodaii str. 7
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96YK1 (Residues: 1-359; Coverage: 100%)
Gene names: STK_21710, mcr, scr
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand PO4 12 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: C2
Unit cell:
a: 167.09Å b: 81.94Å c: 124.61Å
α: 90° β: 104.95° γ: 90°
R-values:
R R work R free
0.187 0.185 0.231
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Unfamiliar metabolic links in the central carbon metabolism.
Fuchs et al. (2014)
9 other articles

3 mentions without citation

Structural basis for a bispecific NADP+ and CoA binding site in an archaeal malonyl-coenzyme A reductase.
Demmer et al. (2013)
2 more