› 4zdc

X-ray diffraction
2.13Å resolution

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, C
Molecule details ›
Chains: A, B, C
Length: 300 amino acids
Theoretical weight: 33.97 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q05871 (Residues: 1-280; Coverage: 100%)
Gene names: ECI1, YLR284C
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1

Ligands and Environments

3 bound ligands:
Ligand SO4 10 x SO4
Ligand CO8 3 x CO8
Ligand GOL 8 x GOL
1 modified residue:
Ligand CME 3 x CME

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P41212
Unit cell:
a: 117.26Å b: 117.26Å c: 219.443Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.168 0.19
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

1 mention without citation

Structure and Mechanism of DHHC Protein Acyltransferases.
Stix et al. (2020)