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AlphaFold monomer V2.0 prediction for common pilus major fimbrillin subunit ecpa (Q8CWB9)

Analyse AlphaFold monomer V2.0 prediction for common pilus major fimbrillin subunit… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q8CWB9
Type: protein
Length: 195 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xaE4667F4997f0196C873a86Bb30DccBBFFD4aE2a
Molecule: Common pilus major fimbrillin subunit ecpa
UniProt: Q8CWB9
Pockets: 1 · best druggability 0.58

Structure

1 distinct chain · 9% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Common pilus major fimbrillin subunit ecpa	protein	195	9% helix, 41% strand	Q8CWB9

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	354	0.58	0.75	42	empty

Compared structures

3QS3 · Crystal structure of the biofilm forming subunit of the E. COLI common pilus: donor… · an experimental structure of the same protein · chain A against H, TM-score 0.78
3QS3 · Crystal structure of the biofilm forming subunit of the E. coli common pilus: donor… · an experimental structure of the same protein · chain A against H, TM-score 0.78

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 Q8CWB9
Elsewhere: UniProt Q8CWB9 · AlphaFold DB Q8CWB9

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