Research workbench
AlphaFold monomer V2.0 prediction for protein translocase subunit seca (A5IM05)
Analyse AlphaFold monomer V2.0 prediction for protein translocase subunit seca (A5IM05) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5IM05
- Type
- protein
- Length
- 871 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4Ef77Afb5a3D9F41c95Be3227D1CC986CCb61835
- Molecule
- Protein translocase subunit seca
- UniProt
- A5IM05
- Pockets
- 9 · best druggability 0.85
Structure
1 distinct chain · 56% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein translocase subunit seca | protein | 871 | 56% helix, 12% strand | A5IM05 |
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1134 | 0.85 | 0.86 | 87 | empty |
| 2 | 923 | 0.73 | 0.77 | 83 | empty |
| 3 | 412 | 0.66 | 0.79 | 57 | empty |
| 4 | 226 | 0.57 | 0.79 | 30 | empty |
| 5 | 111 | 0.50 | 0.81 | 19 | 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 A5IM05
- Elsewhere: UniProt A5IM05 · AlphaFold DB A5IM05
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