2iik

X-ray diffraction
2.55Å resolution

Crystal Structure of human peroxisomal acetyl-CoA acyl transferase 1 (ACAA1)

Released:
Model geometry
Fit model/data
Source organism: Homo sapiens
Entry authors: Papagrigoriou E, Johansson C, Smee C, Kavanagh K, Pike ACW, Sundstrom M, Weigelt J, Edwards A, Arrowsmith CH, Gileadi O, Gorrec F, Umeano C, von Delft F, Oppermann U, Structural Genomics Consortium (SGC)

Function and Biology Details

Reactions catalysed:
Myristoyl-CoA + acetyl-CoA = 3-oxopalmitoyl-CoA + CoA
(1a) [acetyl-CoA C-acyltransferase]-S-acyl-L-cyteine + acetyl-CoA = 3-oxoacyl-CoA + [acetyl-CoA C-acyltransferase]-L-cyteine
(1a) acetyl-CoA + [acetyl-CoA C-acetyltransferase]-L-cysteine = [acetyl-CoA C-acetyltransferase]-S-acetyl-L-cysteine + CoA

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-140554 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-ketoacyl-CoA thiolase, peroxisomal Chains: A, B
Molecule details ›
Chains: A, B
Length: 418 amino acids
Theoretical weight: 43.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P09110 (Residues: 30-424; Coverage: 93%)
Gene names: ACAA, ACAA1, PTHIO
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 55.147Å b: 96.845Å c: 142.055Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.179 0.223
Expression system: Escherichia coli BL21(DE3)