Research workbench
AlphaFold monomer V2.0 prediction for protein translocase subunit seca (A4SEF9)
Analyse AlphaFold monomer V2.0 prediction for protein translocase subunit seca (A4SEF9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A4SEF9
- Type
- protein
- Length
- 1,020 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1ED4a68B4011314730adE976b56Ad4cA21b54dcD
- Molecule
- Protein translocase subunit seca
- UniProt
- A4SEF9
- Pockets
- 7 · best druggability 0.71
Structure
1 distinct chain · 60% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein translocase subunit seca | protein | 1020 | 60% helix, 10% strand | A4SEF9 |
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 525 | 0.71 | 0.80 | 46 | empty |
| 2 | 678 | 0.68 | 0.77 | 61 | empty |
| 3 | 332 | 0.58 | 0.77 | 42 | empty |
| 4 | 354 | 0.58 | 0.76 | 36 | empty |
| 5 | 309 | 0.56 | 0.76 | 35 | 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 A4SEF9
- Elsewhere: UniProt A4SEF9 · AlphaFold DB A4SEF9
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