PDBe 1uys

X-ray diffraction
2.8Å resolution

Acetyl-CoA carboxylase carboxyltransferase domain in complex with inhibitor haloxyfop

Released:

Function and Biology Details

Reactions catalysed:
ATP + biotin-[carboxyl-carrier-protein] + HCO(3)(-) = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein]. 
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
Macromolecule:
Acetyl-CoA carboxylase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 737 amino acids
Theoretical weight: 84.24 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q00955 (Residues: 1482-2218; Coverage: 33%)
Gene names: ABP2, ACC1, FAS3, MTR7, N3175, YNR016C
Sequence domains: Carboxyl transferase domain
Structure domains:

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: C2
Unit cell:
a: 246.21Å b: 125.58Å c: 146.88Å
α: 90° β: 94.08° γ: 90°
R-values:
R R work R free
0.218 0.218 0.252
Expression system: Escherichia coli