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AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (A5FRL3)

Analyse AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (A5FRL3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
A5FRL3
Type
protein
Length
189 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x51B7636bc80cc968e87D857214f08A0195D96382
Molecule
Peptidyl-tRNA hydrolase
UniProt
A5FRL3
Pockets
1 · best druggability 0.45

Structure

1 distinct chain · 45% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidyl-tRNA hydrolaseprotein18945% helix, 23% strandA5FRL3

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11230.450.7728empty

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