X-ray diffraction
2.6Å resolution

Acetyl-CoA carboxylase carboxyltransferase domain L1705I/V1967I mutant


Function and Biology Details

Reactions catalysed:
ATP + [biotin carboxyl-carrier protein]-biotin-N(6)-L-lysine + hydrogencarbonate- = ADP + phosphate + [biotin carboxyl-carrier protein]-carboxybiotin-N(6)-L-lysine
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)
Entry contents:
1 distinct polypeptide molecule
Acetyl-CoA carboxylase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 737 amino acids
Theoretical weight: 83.46 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
  • Canonical: Q00955 (Residues: 1482-2218; Coverage: 33%)
Gene names: ABP2, ACC1, FAS3, MTR7, N3175, YNR016C
Sequence domains: Carboxyl transferase domain
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: C2
Unit cell:
a: 247.17Å b: 123.73Å c: 145.64Å
α: 90° β: 94.2° γ: 90°
R R work R free
0.212 0.212 0.237
Expression system: Escherichia coli