› 3tqx

X-ray diffraction
2.3Å resolution

Structure of the 2-amino-3-ketobutyrate coenzyme A ligase (kbl) from Coxiella burnetii

Released:
DOI: 10.2210/pdb3tqx/pdb
PDB entry 3tqx coloured by chain, front view.
PDB entry 3tqx coloured by chain, side view.
PDB entry 3tqx coloured by chain, top view.
Source organism: Coxiella burnetii RSA 493
Primary publication:
Structural genomics for drug design against the pathogen Coxiella burnetii.
Franklin MC, Cheung J, Rudolph MJ, Burshteyn F, Cassidy M, Gary E, Hillerich B, Yao ZK, Carlier PR, Totrov M, Love JD
Proteins 83 2124-36 (2015)
PMID: 26033498

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182947 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-amino-3-ketobutyrate coenzyme A ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 399 amino acids
Theoretical weight: 44.13 KDa
Source organism: Coxiella burnetii RSA 493
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q83F40 (Residues: 1-396; Coverage: 100%)
Gene names: CBU_0111, kbl
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
No bound ligands
1 modified residue:
Ligand MSE 20 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: C2221
Unit cell:
a: 113.82Å b: 114.85Å c: 136.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.215 0.267
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Laccases of prokaryotic origin: enzymes at the interface of protein science and protein technology.
Martins et al. (2015)
4 more

2 mentions without citation

Type I pyridoxal 5'-phosphate dependent enzymatic domains embedded within multimodular nonribosomal peptide synthetase and polyketide synthase assembly lines.
Milano et al. (2013)
1 more