4asi

X-ray diffraction
2.8Å resolution

Crystal structure of human ACACA C-terminal domain

Released:
Source organism: Homo sapiens
Entry authors: Froese DS, Muniz JRC, Kiyani W, Krojer T, Vollmar M, von Delft F, Bountra C, Arrowsmith CH, Edwards A, Oppermann U, Yue WW

Function and Biology Details

Reaction catalysed:
ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate + malonyl-CoA
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-171524 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetyl-CoA carboxylase 1 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 769 amino acids
Theoretical weight: 87.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q13085 (Residues: 1571-2338; Coverage: 33%)
Gene names: ACAC, ACACA, ACC1, ACCA
Sequence domains: Carboxyl transferase domain
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P212121
Unit cell:
a: 109.966Å b: 143.712Å c: 540.072Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.202 0.236
Expression system: Escherichia coli BL21(DE3)