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AlphaFold monomer V2.0 prediction for trigger factor (Q9RT21)

Analyse AlphaFold monomer V2.0 prediction for trigger factor (Q9RT21) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
Q9RT21
Type
protein
Length
465 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x9B130d619fCFc21d0D08E5Ce38Cf42A5fbe230CB
Molecule
Trigger factor
UniProt
Q9RT21
Pockets
3 · best druggability 0.47

Structure

1 distinct chain · 47% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATrigger factorprotein46547% helix, 17% strandQ9RT21

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11700.470.7615empty
2600.290.7315empty
3500.250.7312empty

Compared structures

  • 2AAR · Structure of trigger factor binding domain in biologically homologous complex with… · an experimental structure of the same protein · chain A against 7, TM-score 0.22
  • 2AAR · Structure of trigger factor binding domain in biologically homologous complex with… · an experimental structure of the same protein · chain A against 7, TM-score 0.22
  • 2D3O · Structure of Ribosome Binding Domain of the Trigger Factor on the 50S ribosomal subunit… · an experimental structure of the same protein · chain A against 1, TM-score 0.17
  • 2D3O · Structure of ribosome binding domain of the trigger factor on the 50S ribosomal subunit… · an experimental structure of the same protein · chain A against 1, TM-score 0.17

Analyse

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