3g8d

X-ray diffraction
1.9Å resolution

Crystal structure of the biotin carboxylase subunit, E296A mutant, of acetyl-COA carboxylase from Escherichia coli

Released:

Function and Biology Details

Reaction catalysed:
ATP + [biotin carboxyl-carrier protein]-biotin-N(6)-L-lysine + hydrogencarbonate- = ADP + phosphate + [biotin carboxyl-carrier protein]-carboxybiotin-N(6)-L-lysine
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150165 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Biotin carboxylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 444 amino acids
Theoretical weight: 48.77 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P24182 (Residues: 1-444; Coverage: 99%)
Gene names: JW3224, accC, b3256, fabG
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P212121
Unit cell:
a: 81.331Å b: 114.738Å c: 122.148Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.198 0.226
Expression system: Escherichia coli