› 6b3t

X-ray diffraction
2.4Å resolution

Crystal structure of acetyltransferase Eis from Mycobacterium tuberculosis in complex with a 1,2,4-triazino[5,6b]indole-3-thioether inhibitor analogue 39b

Released:
DOI: 10.2210/pdb6b3t/pdb
PDB entry 6b3t coloured by chain, front view.
PDB entry 6b3t coloured by chain, side view.
PDB entry 6b3t coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Potent 1,2,4-Triazino[5,6 b]indole-3-thioether Inhibitors of the Kanamycin Resistance Enzyme Eis from Mycobacterium tuberculosis.
Ngo HX, Green KD, Gajadeera CS, Willby MJ, Holbrook SYL, Hou C, Garzan A, Mayhoub AS, Posey JE, Tsodikov OV, Garneau-Tsodikova S
ACS Infect Dis 4 1030-1040 (2018)
PMID: 29601176

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161418 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetyltransferase Eis Chain: A
Molecule details ›
Chain: A
Length: 422 amino acids
Theoretical weight: 46 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WFK7 (Residues: 1-402; Coverage: 100%)
Gene names: MTCY253.04, Rv2416c, eis
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand COA 1 x COA
Ligand CJ7 1 x CJ7
Ligand NA 1 x NA
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: R32
Unit cell:
a: 175.547Å b: 175.547Å c: 120.722Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.217 0.216 0.231
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

The Role of Antibiotic-Target-Modifying and Antibiotic-Modifying Enzymes in Mycobacterium abscessus Drug Resistance.
Luthra et al. (2018)
3 more

3 mentions without citation

An Outline of the Latest Crystallographic Studies on Inhibitor-Enzyme Complexes for the Design and Development of New Therapeutics against Tuberculosis.
Mori et al. (2021)
2 more