› 8i6z

X-ray diffraction
1.95Å resolution

Crystal structure of apo-form of malonyl-CoA reductase C-domain from Chloroflexus aurantiacus

Released:
DOI: 10.2210/pdb8i6z/pdb
PDB entry 8i6z coloured by chain, front view.
PDB entry 8i6z coloured by chain, side view.
PDB entry 8i6z coloured by chain, top view.
Source organism: Chloroflexus aurantiacus
Primary publication:
Cryo-EM structure of bifunctional malonyl-CoA reductase from Chloroflexus aurantiacus reveals a dynamic domain movement for high enzymatic activity.
Ahn JW, Kim S, Hong J, Kim KJ
Int J Biol Macromol 242 124676 (2023)
PMID: 37146856

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-199742 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Short-chain dehydrogenase/reductase SDR Chain: A
Molecule details ›
Chain: A
Length: 689 amino acids
Theoretical weight: 75.35 KDa
Source organism: Chloroflexus aurantiacus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A9WIU3 (Residues: 550-1219; Coverage: 55%)
Gene name: Caur_2614
Sequence domains: short chain dehydrogenase

Ligands and Environments

2 bound ligands:
Ligand GOL 1 x GOL
Ligand TLA 2 x TLA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 7A (6B, 6C1)
Spacegroup: C2
Unit cell:
a: 85.788Å b: 140.355Å c: 73.859Å
α: 90° β: 97.74° γ: 90°
R-values:
R R work R free
0.158 0.156 0.188
Expression system: Escherichia coli BL21(DE3)

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