› 4zdd

X-ray diffraction
3Å resolution

Structure of yeast D3,D2-enoyl-CoA isomerase bound to sulphate ion

Released:
DOI: 10.2210/pdb4zdd/pdb
PDB entry 4zdd coloured by chain, front view.
PDB entry 4zdd coloured by chain, side view.
PDB entry 4zdd coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
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 trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170259 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3,2-trans-enoyl-CoA isomerase Chain: A
Molecule details ›
Chain: A
Length: 300 amino acids
Theoretical weight: 33.89 KDa
Source organism: Saccharomyces cerevisiae S288C
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

1 bound ligand:
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P6322
Unit cell:
a: 116.054Å b: 116.054Å c: 122.096Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.175 0.172 0.223
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