1wdk

X-ray diffraction
2.5Å resolution

fatty acid beta-oxidation multienzyme complex from Pseudomonas fragi, form I (native2)

Released:

Function and Biology Details

Reactions catalysed:
(S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O
(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA
A (3E)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA
(1a) [acetyl-CoA C-acyltransferase]-S-acyl-L-cyteine + acetyl-CoA = 3-oxoacyl-CoA + [acetyl-CoA C-acyltransferase]-L-cyteine
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-151289 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Fatty acid oxidation complex subunit alpha Chains: A, B
Molecule details ›
Chains: A, B
Length: 715 amino acids
Theoretical weight: 77.23 KDa
Source organism: Pseudomonas fragi
Expression system: Escherichia coli
UniProt:
  • Canonical: P28793 (Residues: 1-715; Coverage: 100%)
Gene names: fadB, faoA
Sequence domains:
Structure domains:
3-ketoacyl-CoA thiolase Chains: C, D
Molecule details ›
Chains: C, D
Length: 390 amino acids
Theoretical weight: 41.52 KDa
Source organism: Pseudomonas fragi
Expression system: Escherichia coli
UniProt:
  • Canonical: P28790 (Residues: 2-391; Coverage: 100%)
Gene names: fadA, faoB
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments


Cofactor: Ligand ACO 2 x ACO

Cofactor: Ligand NAD 2 x NAD
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: C2
Unit cell:
a: 180.705Å b: 94.578Å c: 160.001Å
α: 90° β: 111.45° γ: 90°
R-values:
R R work R free
0.206 0.203 0.244
Expression system: Escherichia coli