› 1cwu

X-ray diffraction
2.5Å resolution

BRASSICA NAPUS ENOYL ACP REDUCTASE A138G MUTANT COMPLEXED WITH NAD+ AND THIENODIAZABORINE

Released:
DOI: 10.2210/pdb1cwu/pdb
PDB entry 1cwu coloured by chain, front view.
PDB entry 1cwu coloured by chain, side view.
PDB entry 1cwu coloured by chain, top view.
Source organism: Brassica napus
Primary publication:
Inhibitor binding studies on enoyl reductase reveal conformational changes related to substrate recognition.
Roujeinikova A, Sedelnikova S, de Boer GJ, Stuitje AR, Slabas AR, Rafferty JB, Rice DW
J Biol Chem 274 30811-7 (1999)
PMID: 10521472

Function and Biology Details

Reaction catalysed: 
An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160332 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-[acyl-carrier-protein] reductase [NADH], chloroplastic Chains: A, B
Molecule details ›
Chains: A, B
Length: 296 amino acids
Theoretical weight: 31.32 KDa
Source organism: Brassica napus
Expression system: Escherichia coli
UniProt:
  • Canonical: P80030 (Residues: 85-380; Coverage: 77%)
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
1 bound ligand:
Ligand TDB 2 x TDB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: I4122
Unit cell:
a: 104.58Å b: 104.58Å c: 283.98Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.211 0.314
Expression system: Escherichia coli

Quick links

Citations

11 review citations

The structural biology of type II fatty acid biosynthesis.
White et al. (2005)
10 more

1 mention without citation

Backrub-like backbone simulation recapitulates natural protein conformational variability and improves mutant side-chain prediction.
Smith et al. (2008)