Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent clp protease ATP- binding subunit clpx (A0Q2L0)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent clp protease ATP- binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0Q2L0
- Type
- protein
- Length
- 431 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5A7632cD68306eB5715122da5B344c6126FB602A
- Molecule
- ATP-dependent clp protease ATP-binding subunit clpx
- UniProt
- A0Q2L0
- Pockets
- 5 · best druggability 0.61
Structure
1 distinct chain · 45% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent clp protease ATP-binding subunit clpx | protein | 431 | 45% helix, 13% strand | A0Q2L0 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 250 | 0.61 | 0.80 | 33 | empty |
| 2 | 94 | 0.41 | 0.78 | 22 | empty |
| 3 | 81 | 0.33 | 0.74 | 13 | empty |
| 4 | 78 | 0.32 | 0.74 | 21 | empty |
| 5 | 70 | 0.31 | 0.74 | 19 | 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 A0Q2L0
- Elsewhere: UniProt A0Q2L0 · AlphaFold DB A0Q2L0
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