Research workbench

AlphaFold monomer V2.0 prediction for flagellar P-ring protein (P15930)

Analyse AlphaFold monomer V2.0 prediction for flagellar P-ring protein (P15930) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P15930
Type: protein
Length: 365 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x7c75F0f7d6d136A2b8D4C6C6e9b3D8a697949DF1
UniProt: P15930

Structure

1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	365	—	P15930

Compared structures

7CBL · Cryo-EM structure of the flagellar lp ring from salmonella · an experimental structure of the same protein · chain A against y, TM-score 0.72
7CBL · Cryo-EM structure of the flagellar LP ring from Salmonella · an experimental structure of the same protein · chain A against t, TM-score 0.72

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 P15930
Elsewhere: UniProt P15930 · AlphaFold DB P15930

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