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AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (Q5M222)

Analyse AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (Q5M222) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
Q5M222
Type
protein
Length
189 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x35612D34a32C306CA4fc1edA9360D1F717e25950
Molecule
Peptidyl-tRNA hydrolase
UniProt
Q5M222
Pockets
2 · best druggability 0.36

Structure

1 distinct chain · 44% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidyl-tRNA hydrolaseprotein18944% helix, 25% strandQ5M222

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1700.360.7721empty
2590.270.7318empty

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