› 2cjg

X-ray diffraction
1.95Å resolution

Function and Biology Details

Reaction catalysed: 
L-lysine + 2-oxoglutarate = (S)-2-amino-6-oxohexanoate + L-glutamate
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-162053 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable L-lysine-epsilon aminotransferase Chain: A
Molecule details ›
Chain: A
Length: 449 amino acids
Theoretical weight: 49.07 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WQ77 (Residues: 1-449; Coverage: 100%)
Gene names: MTCY71.30, Rv3290c, lat
Sequence domains: Aminotransferase class-III
Structure domains:

Ligands and Environments


Cofactor: Ligand PMP 1 x PMP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P3121
Unit cell:
a: 103.27Å b: 103.27Å c: 98.266Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.161 0.159 0.186
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Bioinformatic analysis of a PLP-dependent enzyme superfamily suitable for biocatalytic applications.
Steffen-Munsberg et al. (2015)
11 other articles

2 mentions without citation

The pathogenic mechanism of Mycobacterium tuberculosis: implication for new drug development.
Yan et al. (2022)
1 more