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AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (A3MYA5)

Analyse AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (A3MYA5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
A3MYA5
Type
protein
Length
194 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0xB5337bAf208B901b77517FD7A038257Cee30A7e4
Molecule
Peptidyl-tRNA hydrolase
UniProt
A3MYA5
Pockets
1 · best druggability 0.38

Structure

1 distinct chain · 46% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidyl-tRNA hydrolaseprotein19446% helix, 21% strandA3MYA5

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1950.380.7627empty

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