Research workbench

AlphaFold monomer V2.0 prediction for 50S ribosomal protein L19 (Q2YXM4)

Analyse AlphaFold monomer V2.0 prediction for 50S ribosomal protein L19 (Q2YXM4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q2YXM4
Type: protein
Length: 116 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x429aA010A80A47FF4a2777bB34A2bba144d19df2
Molecule: 50S ribosomal protein L19
UniProt: Q2YXM4
Pockets: 1 · best druggability 0.44

Structure

1 distinct chain · 20% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	50S ribosomal protein L19	protein	116	20% helix, 44% strand	Q2YXM4

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	147	0.44	0.76	21	empty

Compared structures

6FXC · The cryo-EM structure of hibernating 100S ribosome dimer from pathogenic Staphylococcus… · an experimental structure of the same protein · chain A against BN, TM-score 0.94
6HMA · Improved model derived from cryo-EM map of Staphylococcus aureus large ribosomal subunit · an experimental structure of the same protein · chain A against N, TM-score 0.93
6HMA · Improved model derived from cryo-EM MAP of staphylococcus aureus large ribosomal subunit · an experimental structure of the same protein · chain A against N, TM-score 0.93

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 Q2YXM4
Elsewhere: UniProt Q2YXM4 · AlphaFold DB Q2YXM4

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