› 2w6o

X-ray diffraction
2.5Å resolution

Crystal structure of Biotin carboxylase from E. coli in complex with 4-Amino-7,7-dimethyl-7,8-dihydro-quinazolinone fragment

Released:
DOI: 10.2210/pdb2w6o/pdb
PDB entry 2w6o coloured by chain, front view.
PDB entry 2w6o coloured by chain, side view.
PDB entry 2w6o coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Discovery of antibacterial biotin carboxylase inhibitors by virtual screening and fragment-based approaches.
Mochalkin I, Miller JR, Narasimhan L, Thanabal V, Erdman P, Cox PB, Prasad JV, Lightle S, Huband MD, Stover CK
ACS Chem Biol 4 473-83 (2009)
PMID: 19413326

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:
Biological process:
Cellular component:
Sequence domains:

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, C
Molecule details ›
Chains: A, C
Length: 449 amino acids
Theoretical weight: 49.39 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

2 bound ligands:
Ligand OA3 2 x OA3
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 68.629Å b: 113.367Å c: 121.737Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.234 0.23 0.308
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Structure and function of biotin-dependent carboxylases.
Tong L. (2013)
15 more

1 mention without citation

Computational redesign of bacterial biotin carboxylase inhibitors using structure-based virtual screening of combinatorial libraries.
Brylinski et al. (2014)