4k3w

X-ray diffraction
2.31Å resolution

Crystal structure of an enoyl-CoA hydratase/isomerase from Marinobacter aquaeolei

Released:
Source organism: Marinobacter nauticus VT8
Entry authors: Eswaramoorthy S, Chamala S, Evans B, Foti F, Gizzi A, Hillerich B, Kar A, Lafleur J, Seidel R, Villigas G, Zencheck W, Al Obaidi N, Almo SC, Swaminathan S, New York Structural Genomics Research Consortium (NYSGRC)

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-106720 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-CoA hydratase/isomerase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 296 amino acids
Theoretical weight: 32.43 KDa
Source organism: Marinobacter nauticus VT8
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: A1U4G2 (Residues: 1-274; Coverage: 100%)
Gene name: Maqu_2806
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2
Unit cell:
a: 232.355Å b: 135.143Å c: 43.042Å
α: 90° β: 99.09° γ: 90°
R-values:
R R work R free
0.197 0.195 0.227
Expression system: Escherichia coli BL21