MolNFT v1 · #319395 · protein

AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (A5F686)

A5F686: “AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (A5F686)”. 1 pocket (best druggability 0.41). MolNFT v1 #319395 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

Accession: A5F686
Type: protein
Length: 196 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x71112d4fF7ebb3b617963c05f052289e073082FD
Molecule: Peptidyl-tRNA hydrolase
UniProt: A5F686
Pockets: 1 · best druggability 0.41

Structure

1 distinct chain · 44% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-tRNA hydrolase	protein	196	44% helix, 22% strand	A5F686

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	67	0.41	0.81	21	empty

Compared structures

5B6J · Crystal structure of peptidyl-tRNA hydrolase mutant -H24N from vibrio cholerae · an experimental structure of the same protein · chain A against A, TM-score 0.99
5B6J · Crystal structure of Peptidyl-tRNA hydrolase mutant -H24N from Vibrio cholerae · an experimental structure of the same protein · chain A against A, TM-score 0.99
5GVZ · Crystal structure of peptidyl-tRNA hydrolase from vibrio cholerae in space group C2221 at… · an experimental structure of the same protein · chain A against A, TM-score 0.98
5GVZ · Crystal structure of Peptidyl-tRNA hydrolase from Vibrio cholerae in space group C2221 at… · an experimental structure of the same protein · chain A against A, TM-score 0.98

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 A5F686
Elsewhere: UniProt A5F686 · AlphaFold DB A5F686

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