Research workbench
AlphaFold monomer V2.0 prediction for protein translocase subunit seca (Q1RG97)
Analyse AlphaFold monomer V2.0 prediction for protein translocase subunit seca (Q1RG97) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q1RG97
- Type
- protein
- Length
- 901 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc7289c3ff1CD901cF20482f898aA0720155C409f
- Molecule
- Protein translocase subunit seca
- UniProt
- Q1RG97
- Pockets
- 10 · best druggability 0.80
Structure
1 distinct chain · 58% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein translocase subunit seca | protein | 901 | 58% helix, 11% strand | Q1RG97 |
Pockets
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1031 | 0.80 | 0.81 | 112 | empty |
| 2 | 123 | 0.64 | 0.87 | 21 | empty |
| 3 | 454 | 0.63 | 0.77 | 48 | empty |
| 4 | 282 | 0.58 | 0.78 | 37 | empty |
| 5 | 319 | 0.54 | 0.74 | 27 | 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 Q1RG97
- Elsewhere: UniProt Q1RG97 · AlphaFold DB Q1RG97
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