Research workbench
AlphaFold monomer V2.0 prediction for outer membrane protein P1 (P10641)
Analyse AlphaFold monomer V2.0 prediction for outer membrane protein P1 (P10641) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P10641
- Type
- protein
- Length
- 459 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa73BAb1DabE4333A884D03393eAa10c3B4215494
- Molecule
- Outer membrane protein P1
- UniProt
- P10641
- Pockets
- 6 · best druggability 0.76
Structure
1 distinct chain · 10% helix, 59% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Outer membrane protein P1 | protein | 459 | 10% helix, 59% strand | P10641 |
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 86 | 0.76 | 0.97 | 24 | empty |
| 2 | 67 | 0.72 | 0.98 | 25 | empty |
| 3 | 187 | 0.68 | 0.87 | 33 | empty |
| 4 | 348 | 0.60 | 0.77 | 40 | empty |
| 5 | 127 | 0.58 | 0.84 | 28 | empty |
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 P10641
- Elsewhere: UniProt P10641 · AlphaFold DB P10641
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