› 1fc4

X-ray diffraction
2Å resolution

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + glycine = CoA + 2-amino-3-oxobutanoate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142020 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-amino-3-ketobutyrate coenzyme A ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 401 amino acids
Theoretical weight: 44.01 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P0AB77 (Residues: 1-398; Coverage: 100%)
Gene names: JW3592, b3617, kbl
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
1 bound ligand:
Ligand AKB 2 x AKB
1 modified residue:
Ligand MSE 24 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P212121
Unit cell:
a: 63.936Å b: 98.659Å c: 118.699Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.151 0.151 0.212
Expression system: Not provided

Quick links

Citations

6 review citations

Biotin in microbes, the genes involved in its biosynthesis, its biochemical role and perspectives for biotechnological production.
Streit et al. (2003)
5 more

11 mentions without citation

Contribution of structural genomics to understanding the biology of Escherichia coli.
Matte et al. (2003)
10 more