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Crystal structure of TACT3 (tRNA acetylating toxin) from salmonella

Analyse Crystal structure of TACT3 (tRNA acetylating toxin) from salmonella in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6G96
Type
protein
Length
349 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Acetyltransferase
UniProt
A0A0J5HSJ5
Ligands
ACO, BCN
Pockets
4 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
BAcetyltransferaseprotein17434% helix, 33% strandA0A0J5HSJ5
AAcetyltransferaseprotein17537% helix, 27% strandA0A0J5HSJ5

Ligands and binding sites

  • ACO · Acetyl coenzyme *A · ligand · 2 copies · chains B, A
  • BCN · Bicine · ligand · chains B
  • GOL · Glycerol · additive · 2 copies · chains B, A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17370.710.7766ACO
24590.660.7846ACO
31370.420.7418GOL
4580.270.7416empty

Interfaces

1 interface between chains.

  • B–A · 1109 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 6G96 · Crystal structure of TacT3 (tRNA acetylating toxin) from Salmonella · the same entry in another collection · chain B against B, TM-score 1.00

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