2yl2

X-ray diffraction
2.3Å resolution

Crystal structure of human acetyl-CoA carboxylase 1, biotin carboxylase (BC) domain

Released:
Source organism: Homo sapiens
Entry authors: Muniz JRC, Froese DS, Krysztofinska E, Vollmar M, Beltrami A, Krojer T, von Delft F, Arrowsmith CH, Edwards AM, Weigelt J, Bountra C, Yue WW, Oppermann U

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:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-171523 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetyl-CoA carboxylase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 540 amino acids
Theoretical weight: 60.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q13085 (Residues: 78-617; Coverage: 23%)
Gene names: ACAC, ACACA, ACC1, ACCA
Sequence domains:
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: P1
Unit cell:
a: 60.67Å b: 60.87Å c: 70.37Å
α: 92.04° β: 98° γ: 92.2°
R-values:
R R work R free
0.208 0.206 0.241
Expression system: Escherichia coli BL21(DE3)