› 7kz3

X-ray diffraction
1.55Å resolution

Crystal structure of KabA from Bacillus cereus UW85 in complex with the internal aldimine

Released:
DOI: 10.2210/pdb7kz3/pdb
PDB entry 7kz3 coloured by chain, front view.
PDB entry 7kz3 coloured by chain, side view.
PDB entry 7kz3 coloured by chain, top view.
Source organism: Bacillus cereus
Primary publication:
Snapshots along the catalytic path of KabA, a PLP-dependent aminotransferase required for kanosamine biosynthesis in Bacillus cereus UW85.
Prasertanan T, Palmer DRJ, Sanders DAR
J Struct Biol 213 107744 (2021)
PMID: 33984505

Function and Biology Details

Reaction catalysed: 
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110990 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
KabA Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 445 amino acids
Theoretical weight: 51.21 KDa
Source organism: Bacillus cereus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: C0JRF5 (Residues: 1-441; Coverage: 100%)
Gene names: GE376_30835, kabA
Sequence domains: DegT/DnrJ/EryC1/StrS aminotransferase family

Ligands and Environments

2 bound ligands:
Ligand EDO 69 x EDO
Ligand NA 2 x NA
1 modified residue:
Ligand LLP 4 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P1
Unit cell:
a: 66.46Å b: 66.68Å c: 111.83Å
α: 81.08° β: 77.41° γ: 88.05°
R-values:
R R work R free
0.151 0.15 0.181
Expression system: Escherichia coli BL21

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Citations

1 citations in other articles

Conformational change of organic cofactor PLP is essential for catalysis in PLP-dependent enzymes.
Ngo et al. (2022)