2gpw

X-ray diffraction
2.2Å resolution

Crystal Structure of the Biotin Carboxylase Subunit, F363A Mutant, of Acetyl-CoA Carboxylase from Escherichia coli.

Released:
Source organism: Escherichia coli

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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 469 amino acids
Theoretical weight: 51.48 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P24182 (Residues: 1-449; Coverage: 100%)
Gene names: JW3224, accC, b3256, fabG
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P21
Unit cell:
a: 62.351Å b: 81.499Å c: 176.649Å
α: 90° β: 97.69° γ: 90°
R-values:
R R work R free
0.192 0.192 0.25
Expression system: Escherichia coli