Research workbench
AlphaFold monomer V2.0 prediction for protein translocase subunit seca (Q65VS6)
Analyse AlphaFold monomer V2.0 prediction for protein translocase subunit seca (Q65VS6) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q65VS6
- Type
- protein
- Length
- 896 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7c75F0f7d6d136A2b8D4C6C6e9b3D8a697949DF1
- Molecule
- Protein translocase subunit seca
- UniProt
- Q65VS6
- Pockets
- 7 · best druggability 0.67
Structure
1 distinct chain · 56% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein translocase subunit seca | protein | 896 | 56% helix, 12% strand | Q65VS6 |
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 551 | 0.67 | 0.77 | 45 | empty |
| 2 | 332 | 0.62 | 0.79 | 42 | empty |
| 3 | 208 | 0.56 | 0.79 | 41 | empty |
| 4 | 123 | 0.50 | 0.81 | 26 | empty |
| 5 | 150 | 0.43 | 0.75 | 15 | 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 Q65VS6
- Elsewhere: UniProt Q65VS6 · AlphaFold DB Q65VS6
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