Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent zinc metalloprotease ftsh (Q0TTK8)
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
- Q0TTK8
- Type
- protein
- Length
- 717 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x79a905d858Ce72991FD6E7a9C6498620f42E146D
- Molecule
- ATP-dependent zinc metalloprotease ftsh
- UniProt
- Q0TTK8
- Pockets
- 6 · best druggability 0.66
Structure
1 distinct chain · 57% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent zinc metalloprotease ftsh | protein | 717 | 57% helix, 12% strand | Q0TTK8 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 485 | 0.66 | 0.78 | 55 | empty |
| 2 | 661 | 0.65 | 0.75 | 61 | empty |
| 3 | 347 | 0.53 | 0.74 | 36 | empty |
| 4 | 80 | 0.46 | 0.81 | 15 | empty |
| 5 | 57 | 0.38 | 0.80 | 14 | 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 Q0TTK8
- Elsewhere: UniProt Q0TTK8 · AlphaFold DB Q0TTK8
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