Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent zinc metalloprotease ftsh (O83746)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent zinc metalloprotease ftsh… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O83746
- Type
- protein
- Length
- 609 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3298b100681D3A2372Bba3b2f282750dD71629B9
- Molecule
- ATP-dependent zinc metalloprotease ftsh
- UniProt
- O83746
- Pockets
- 6 · best druggability 0.67
Structure
1 distinct chain · 49% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent zinc metalloprotease ftsh | protein | 609 | 49% helix, 12% strand | O83746 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 567 | 0.67 | 0.77 | 59 | empty |
| 2 | 58 | 0.45 | 0.83 | 20 | empty |
| 3 | 87 | 0.39 | 0.77 | 15 | empty |
| 4 | 62 | 0.37 | 0.78 | 13 | empty |
| 5 | 98 | 0.33 | 0.73 | 18 | 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 O83746
- Elsewhere: UniProt O83746 · AlphaFold DB O83746
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