2j5i

X-ray diffraction
1.8Å resolution

Function and Biology Details

Reaction catalysed:
(1a) feruloyl-CoA + H(2)O = 3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Hydroxycinnamoyl-CoA hydratase-lyase Chain: A
Molecule details ›
Chain: A
Length: 276 amino acids
Theoretical weight: 31.01 KDa
Source organism: Pseudomonas fluorescens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O69762 (Residues: 1-276; Coverage: 100%)
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:
Hydroxycinnamoyl-CoA hydratase-lyase Chains: B, C, D, E, F, G, H, J, K, L
Molecule details ›
Chains: B, C, D, E, F, G, H, J, K, L
Length: 276 amino acids
Theoretical weight: 31.04 KDa
Source organism: Pseudomonas fluorescens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O69762 (Residues: 1-276; Coverage: 100%)
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:
Hydroxycinnamoyl-CoA hydratase-lyase Chain: I
Molecule details ›
Chain: I
Length: 276 amino acids
Theoretical weight: 31.04 KDa
Source organism: Pseudomonas fluorescens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O69762 (Residues: 1-276; Coverage: 100%)
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21212
Unit cell:
a: 154.238Å b: 167.487Å c: 130.818Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.179 0.215
Expression system: Escherichia coli BL21(DE3)