Research workbench

P15928: AlphaFold monomer V2.0 prediction for flagellar M-ring protein (P15928)

Analyse P15928: AlphaFold monomer V2.0 prediction for flagellar M-ring protein (P15928) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P15928
Type: protein
Length: 560 residues
Chains: 1
Deposited: 09-DEC-21
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x2E07DDd2cabd9424b49B257870F758CE578010E0
Molecule: Flagellar M-ring protein
UniProt: P15928
Pockets: 2 · best druggability 0.35

Structure

1 distinct chain · 40% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Flagellar M-ring protein	protein	560	40% helix, 18% strand	P15928

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	106	0.35	0.74	20	empty
2	59	0.27	0.73	14	empty

Compared structures

8ZDS · Structure of the Salmonella flagellar MS-ring with C11 symmetry applied · an experimental structure of the same protein · chain A against R, TM-score 0.36
8T8P · 33-mer FliF MS-ring from Salmonella · an experimental structure of the same protein · chain A against A, TM-score 0.36

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 P15928
Elsewhere: UniProt P15928 · AlphaFold DB P15928

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