› 4zdf

X-ray diffraction
1.81Å resolution

Crystal structure of yeast enoyl-CoA isomerase helix-10 deletion (ScECI2-H10) mutant

Released:
DOI: 10.2210/pdb4zdf/pdb
PDB entry 4zdf coloured by chain, front view.
PDB entry 4zdf coloured by chain, side view.
PDB entry 4zdf coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structures of yeast peroxisomal Δ(3),Δ(2)-enoyl-CoA isomerase complexed with acyl-CoA substrate analogues: the importance of hydrogen-bond networks for the reactivity of the catalytic base and the oxyanion hole.
Onwukwe GU, Koski MK, Pihko P, Schmitz W, Wierenga RK
Acta Crystallogr D Biol Crystallogr 71 2178-91 (2015)
PMID: 26527136

Function and Biology Details

Reaction catalysed: 
A (3E)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170260 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3,2-trans-enoyl-CoA isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 288 amino acids
Theoretical weight: 32.47 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q05871 (Residues: 1-268; Coverage: 96%)
Gene names: ECI1, YLR284C
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1

Ligands and Environments

1 bound ligand:
Ligand GOL 1 x GOL
1 modified residue:
Ligand CME 2 x CME

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P321
Unit cell:
a: 118.121Å b: 118.121Å c: 87.417Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.161 0.159 0.188
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Carboxylate Catalyzed Isomerization of β,γ-Unsaturated N-Acetylcysteamine Thioesters.
Riuttamäki et al. (2022)
1 more