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AlphaFold monomer V2.0 prediction for accessory sec system protein translocase subunit SECY2 (F8LR08)
Analyse AlphaFold monomer V2.0 prediction for accessory sec system protein translocase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- F8LR08
- Type
- protein
- Length
- 408 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x661f92Fc5950020C7aB410B5F5b9a3f429F49Ae5
- Molecule
- Accessory sec system protein translocase subunit SECY2
- UniProt
- F8LR08
- Pockets
- 4 · best druggability 0.56
Structure
1 distinct chain · 74% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Accessory sec system protein translocase subunit SECY2 | protein | 408 | 74% helix, 5% strand | F8LR08 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 230 | 0.56 | 0.78 | 41 | empty |
| 2 | 136 | 0.51 | 0.79 | 23 | empty |
| 3 | 116 | 0.42 | 0.76 | 22 | empty |
| 4 | 134 | 0.39 | 0.74 | 22 | 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 F8LR08
- Elsewhere: UniProt F8LR08 · AlphaFold DB F8LR08
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