› 1guf

X-ray diffraction
2.25Å resolution

Enoyl thioester reductase from Candida tropicalis

Released:
DOI: 10.2210/pdb1guf/pdb
PDB entry 1guf coloured by chain, front view.
PDB entry 1guf coloured by chain, side view.
PDB entry 1guf coloured by chain, top view.
Source organism: Candida tropicalis
Primary publication:
Structure-function analysis of enoyl thioester reductase involved in mitochondrial maintenance.
Airenne TT, Torkko JM, Van den plas S, Sormunen RT, Kastaniotis AJ, Wierenga RK, Hiltunen JK
J Mol Biol 327 47-59 (2003)
PMID: 12614607

Function and Biology Details

Reaction catalysed: 
An acyl-[acyl-carrier protein] + NADP(+) = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186819 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-[acyl-carrier-protein] reductase 1, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 364 amino acids
Theoretical weight: 39.56 KDa
Source organism: Candida tropicalis
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: Q8WZM3 (Residues: 23-386; Coverage: 94%)
Gene name: ETR1
Sequence domains: Zinc-binding dehydrogenase
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand GOL 5 x GOL
Ligand SO4 8 x SO4
Ligand NDP 2 x NDP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P3121
Unit cell:
a: 92.17Å b: 92.17Å c: 225.66Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.178 0.178 0.215
Expression system: Saccharomyces cerevisiae

Quick links

Citations

6 review citations

Fatty acid synthesis and elongation in yeast.
Tehlivets et al. (2007)
5 more

6 mentions without citation

Divergence of multimodular polyketide synthases revealed by a didomain structure.
Zheng et al. (2012)
5 more