Research workbench
AlphaFold monomer V2.0 prediction for protein translocase subunit seca (A5EY15)
Analyse AlphaFold monomer V2.0 prediction for protein translocase subunit seca (A5EY15) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5EY15
- Type
- protein
- Length
- 906 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0EA189b2343A464f560b44103f6A3396Da1dA8a9
- Molecule
- Protein translocase subunit seca
- UniProt
- A5EY15
- Pockets
- 5 · best druggability 0.67
Structure
1 distinct chain · 55% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein translocase subunit seca | protein | 906 | 55% helix, 11% strand | A5EY15 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 588 | 0.67 | 0.77 | 43 | empty |
| 2 | 430 | 0.64 | 0.78 | 56 | empty |
| 3 | 154 | 0.47 | 0.77 | 27 | empty |
| 4 | 106 | 0.44 | 0.79 | 25 | empty |
| 5 | 141 | 0.44 | 0.76 | 20 | 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 A5EY15
- Elsewhere: UniProt A5EY15 · AlphaFold DB A5EY15
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