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AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (A5F686)

Analyse AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (A5F686) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
A5F686
Type
protein
Length
196 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x71112d4fF7ebb3b617963c05f052289e073082FD
Molecule
Peptidyl-tRNA hydrolase
UniProt
A5F686
Pockets
1 · best druggability 0.41

Structure

1 distinct chain · 44% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidyl-tRNA hydrolaseprotein19644% helix, 22% strandA5F686

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1670.410.8121empty

Compared structures

  • 5B6J · Crystal structure of peptidyl-tRNA hydrolase mutant -H24N from vibrio cholerae · an experimental structure of the same protein · chain A against A, TM-score 0.99
  • 5B6J · Crystal structure of Peptidyl-tRNA hydrolase mutant -H24N from Vibrio cholerae · an experimental structure of the same protein · chain A against A, TM-score 0.99
  • 5GVZ · Crystal structure of peptidyl-tRNA hydrolase from vibrio cholerae in space group C2221 at… · an experimental structure of the same protein · chain A against A, TM-score 0.98
  • 5GVZ · Crystal structure of Peptidyl-tRNA hydrolase from Vibrio cholerae in space group C2221 at… · an experimental structure of the same protein · chain A against A, TM-score 0.98

Analyse

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