› 1od4

X-ray diffraction
2.7Å resolution

Acetyl-CoA Carboxylase Carboxyltransferase Domain

Released:
DOI: 10.2210/pdb1od4/pdb
PDB entry 1od4 coloured by chain, front view.
PDB entry 1od4 coloured by chain, side view.
PDB entry 1od4 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase.
Zhang H, Yang Z, Shen Y, Tong L
Science 299 2064-7 (2003)
PMID: 12663926

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:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169488 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetyl-CoA carboxylase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 805 amino acids
Theoretical weight: 91.99 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q00955 (Residues: 1429-2233; Coverage: 36%)
Gene names: ABP2, ACC1, FAS3, MTR7, N3175, YNR016C
Sequence domains: Carboxyl transferase domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ADE 1 x ADE
1 modified residue:
Ligand MSE 60 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: C2
Unit cell:
a: 246.91Å b: 123.91Å c: 145.07Å
α: 90° β: 94.11° γ: 90°
R-values:
R R work R free
0.226 0.226 0.262
Expression system: Escherichia coli

Quick links

Citations

22 review citations

Evolution in action: plants resistant to herbicides.
Powles et al. (2010)
21 more

1 mention without citation

An asymmetric model for Na+-translocating glutaconyl-CoA decarboxylases.
Kress et al. (2009)