MolNFT v1 · #423989 · protein
AlphaFold monomer V2.0 prediction for protein translocase subunit seca (A5VIG0)
A5VIG0: “AlphaFold monomer V2.0 prediction for protein translocase subunit seca (A5VIG0)”. 9 pockets (best druggability 0.59). MolNFT v1 #423989 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- A5VIG0
- Type
- protein
- Length
- 787 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xA9CF663CecE9dfC23a2306df169ba1dA3b6d6CD5
- Molecule
- Protein translocase subunit seca
- UniProt
- A5VIG0
- Pockets
- 9 · best druggability 0.59
Structure
1 distinct chain · 57% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein translocase subunit seca | protein | 787 | 57% helix, 12% strand | A5VIG0 |
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 | 315 | 0.59 | 0.78 | 37 | empty |
| 2 | 218 | 0.54 | 0.78 | 32 | empty |
| 3 | 108 | 0.54 | 0.82 | 18 | empty |
| 4 | 226 | 0.52 | 0.77 | 29 | empty |
| 5 | 117 | 0.45 | 0.78 | 25 | 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 A5VIG0
- Elsewhere: UniProt A5VIG0 · AlphaFold DB A5VIG0
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