› 1d7o

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF BRASSICA NAPUS ENOYL ACYL CARRIER PROTEIN REDUCTASE COMPLEXED WITH NAD AND TRICLOSAN

Released:
DOI: 10.2210/pdb1d7o/pdb
PDB entry 1d7o coloured by chain, front view.
PDB entry 1d7o coloured by chain, side view.
PDB entry 1d7o coloured by chain, top view.
Source organism: Brassica napus
Primary publication:
Crystallographic analysis of triclosan bound to enoyl reductase.
Roujeinikova A, Levy CW, Rowsell S, Sedelnikova S, Baker PJ, Minshull CA, Mistry A, Colls JG, Camble R, Stuitje AR, Slabas AR, Rafferty JB, Pauptit RA, Viner R, Rice DW
J Mol Biol 294 527-35 (1999)
PMID: 10610777

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 Chain: A
Molecule details ›
Chain: A
Length: 297 amino acids
Theoretical weight: 31.39 KDa
Source organism: Brassica napus
Expression system: Escherichia coli
UniProt:
  • Canonical: P80030 (Residues: 84-380; Coverage: 77%)
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAD 1 x NAD
1 bound ligand:
Ligand TCL 1 x TCL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P42212
Unit cell:
a: 70.5Å b: 70.5Å c: 118Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.162 0.225
Expression system: Escherichia coli

Quick links

Citations

13 review citations

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

4 mentions without citation

Correspondences between low-energy modes in enzymes: dynamics-based alignment of enzymatic functional families.
Zen et al. (2008)
3 more