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AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (Q92N67)

Analyse AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (Q92N67) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
Q92N67
Type
protein
Length
239 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0xf87a97E0A4bB354D834857B14296240B167cbe70
Molecule
Peptidyl-tRNA hydrolase
UniProt
Q92N67
Pockets
1 · best druggability 0.36

Structure

1 distinct chain · 40% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidyl-tRNA hydrolaseprotein23940% helix, 18% strandQ92N67

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1830.360.7619empty

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