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› 7bxq

X-ray diffraction
2.49Å resolution

2-amino-3-ketobutyrate CoA ligase from Cupriavidus necator L-Threonine binding form

Released:
DOI: 10.2210/pdb7bxq/pdb
Model geometry
Fit model/data
PDB entry 7bxq coloured by chain, front view.
PDB entry 7bxq coloured by chain, side view.
PDB entry 7bxq coloured by chain, top view.
Source organism: Cupriavidus necator
Primary publication:
Chemoenzymatic synthesis of 3-ethyl-2,5-dimethylpyrazine by L-threonine 3-dehydrogenase and 2-amino-3-ketobutyrate CoA ligase/L-threonine aldolase
Motoyama T, Nakano S, Hasebe F, Miyata R, Kumazawa S, Miyoshi N, Ito S
Commun Chem 4 108-108 (2021)

Function and Biology Details

Reaction catalysed: 
glycine + acetyl-CoA = (2S)-2-amino-3-oxobutanoate + CoA.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170975 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-amino-3-ketobutyrate coenzyme A ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 411 amino acids
Theoretical weight: 44.79 KDa
Source organism: Cupriavidus necator
Expression system: Escherichia coli
UniProt:
  • Canonical: Q0K313 (Residues: 1-399; Coverage: 100%)
Gene names: E6A55_23280, H16_B0819, kbl
Sequence domains: Aminotransferase class I and II

Ligands and Environments

1 bound ligand:
Ligand 2BK 2 x 2BK
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P21
Unit cell:
a: 58.708Å b: 101.657Å c: 69.854Å
α: 90° β: 112.99° γ: 90°
R-values:
R R work R free
0.188 0.185 0.258
Expression system: Escherichia coli

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