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AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (A3PML9)

Analyse AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (A3PML9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: A3PML9
Type: protein
Length: 225 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xbDA05C32aD6eE153C8C5A78dfa48d7Ba25694fea
Molecule: Peptidyl-tRNA hydrolase
UniProt: A3PML9
Pockets: 2 · best druggability 0.34

Structure

1 distinct chain · 43% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-tRNA hydrolase	protein	225	43% helix, 20% strand	A3PML9

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	55	0.34	0.78	16	empty
2	53	0.27	0.74	16	empty

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt A3PML9
Elsewhere: UniProt A3PML9 · AlphaFold DB A3PML9

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