1bdo

X-ray diffraction
1.8Å resolution

STRUCTURE OF THE BIOTINYL DOMAIN OF ACETYL-COENZYME A CARBOXYLASE DETERMINED BY MAD PHASING

Released:

Function and Biology Details

Reaction catalysed:
ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate + malonyl-CoA
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Biotin carboxyl carrier protein of acetyl-CoA carboxylase Chain: A
Molecule details ›
Chain: A
Length: 80 amino acids
Theoretical weight: 8.7 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ABD8 (Residues: 77-156; Coverage: 51%)
Gene names: JW3223, accB, b3255, fabE
Sequence domains: Biotin-requiring enzyme
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)

Ligands and Environments


Cofactor: Ligand BTN 1 x BTN
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P21212
Unit cell:
a: 65.46Å b: 37.26Å c: 35.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 not available
Expression system: Escherichia coli