PDBe 2bdo

Solution NMR

SOLUTION STRUCTURE OF HOLO-BIOTINYL DOMAIN FROM ACETYL COENZYME A CARBOXYLASE OF ESCHERICHIA COLI DETERMINED BY TRIPLE-RESONANCE NMR SPECTROSCOPY

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:
monomeric (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 BL21(DE3)
Expression system: Escherichia coli BL21(DE3)
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

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 82%
Chemical shifts: BMR4426  
Expression system: Escherichia coli BL21(DE3)