Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent protease ATPase subunit hslu (C3L798)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent protease ATPase subunit… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C3L798
- Type
- protein
- Length
- 463 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB44F19a0cb161828322eEEd13F55d4C3C34938d2
- Molecule
- ATP-dependent protease ATPase subunit hslu
- UniProt
- C3L798
- Pockets
- 4 · best druggability 0.64
Structure
1 distinct chain · 56% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent protease ATPase subunit hslu | protein | 463 | 56% helix, 12% strand | C3L798 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 332 | 0.64 | 0.80 | 41 | empty |
| 2 | 75 | 0.37 | 0.77 | 14 | empty |
| 3 | 114 | 0.37 | 0.73 | 16 | empty |
| 4 | 57 | 0.31 | 0.76 | 13 | 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 C3L798
- Elsewhere: UniProt C3L798 · AlphaFold DB C3L798
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