› 1pn2

X-ray diffraction
1.95Å resolution

Crystal structure analysis of the selenomethionine labelled 2-enoyl-CoA hydratase 2 domain of Candida tropicalis multifunctional enzyme type 2

Released:
DOI: 10.2210/pdb1pn2/pdb
PDB entry 1pn2 coloured by chain, front view.
PDB entry 1pn2 coloured by chain, side view.
PDB entry 1pn2 coloured by chain, top view.
Source organism: Candida tropicalis
Primary publication:
A two-domain structure of one subunit explains unique features of eukaryotic hydratase 2.
Koski MK, Haapalainen AM, Hiltunen JK, Glumoff T
J Biol Chem 279 24666-72 (2004)
PMID: 15051722

Function and Biology Details

Reactions catalysed: 
(R)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH
(3R)-3-hydroxyacyl-CoA = (2E)-2-enoyl-CoA + H(2)O
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149628 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxisomal hydratase-dehydrogenase-epimerase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 280 amino acids
Theoretical weight: 31.59 KDa
Source organism: Candida tropicalis
Expression system: Escherichia coli
UniProt:
  • Canonical: P22414 (Residues: 627-906; Coverage: 31%)
Sequence domains: MaoC like domain
Structure domains: Hotdog Thioesterase

Ligands and Environments

1 bound ligand:
Ligand EDO 5 x EDO
1 modified residue:
Ligand MSE 16 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: C2
Unit cell:
a: 178.8Å b: 60.648Å c: 131.117Å
α: 90° β: 94.571° γ: 90°
R-values:
R R work R free
0.182 0.179 0.214
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Peroxisomal beta-oxidation--a metabolic pathway with multiple functions.
Poirier et al. (2006)
6 more

9 mentions without citation

Active site comparisons and catalytic mechanisms of the hot dog superfamily.
Labonte et al. (2013)
8 more