Research workbench
AlphaFold monomer V2.0 prediction for motility protein B (P28612)
Analyse AlphaFold monomer V2.0 prediction for motility protein B (P28612) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P28612
- Type
- protein
- Length
- 261 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xA05C03312A50fd47Fd710A12DeAaAB1Df3db1bCA
- Molecule
- Motility protein B
- UniProt
- P28612
- Pockets
- 1 · best druggability 0.28
Structure
1 distinct chain · 49% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Motility protein B | protein | 261 | 49% helix, 12% strand | P28612 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.28 | 0.75 | 15 | empty |
Compared structures
- 6YSL · Structure of the flagellar motab stator complex from bacillus subtilis · an experimental structure of the same protein · chain A against A, TM-score 0.10
- 6YSL · Structure of the flagellar MotAB stator complex from Bacillus subtilis · an experimental structure of the same protein · chain A against A, TM-score 0.10
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 P28612
- Elsewhere: UniProt P28612 · AlphaFold DB P28612
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