Research workbench
AlphaFold monomer V2.0 prediction for protein translocase subunit seca (B5ELD9)
Analyse AlphaFold monomer V2.0 prediction for protein translocase subunit seca (B5ELD9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5ELD9
- Type
- protein
- Length
- 914 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x827Dcb147886372317f263288bc31c7eeFc7876c
- Molecule
- Protein translocase subunit seca
- UniProt
- B5ELD9
- Pockets
- 7 · best druggability 0.77
Structure
1 distinct chain · 55% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein translocase subunit seca | protein | 914 | 55% helix, 11% strand | B5ELD9 |
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 | 1064 | 0.77 | 0.79 | 109 | empty |
| 2 | 365 | 0.66 | 0.80 | 44 | empty |
| 3 | 543 | 0.66 | 0.77 | 44 | empty |
| 4 | 92 | 0.60 | 0.88 | 20 | empty |
| 5 | 175 | 0.52 | 0.79 | 32 | 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 B5ELD9
- Elsewhere: UniProt B5ELD9 · AlphaFold DB B5ELD9
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