Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent clp protease ATP- binding subunit clpx (A0LSV2)
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
- A0LSV2
- Type
- protein
- Length
- 427 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x2Fc9Fe89158bF2facca1427c2b13b0cEc88Aaa5a
- Molecule
- ATP-dependent clp protease ATP-binding subunit clpx
- UniProt
- A0LSV2
- Pockets
- 5 · best druggability 0.58
Structure
1 distinct chain · 47% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent clp protease ATP-binding subunit clpx | protein | 427 | 47% helix, 14% strand | A0LSV2 |
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 | 271 | 0.58 | 0.78 | 31 | empty |
| 2 | 93 | 0.35 | 0.74 | 16 | empty |
| 3 | 61 | 0.32 | 0.76 | 14 | empty |
| 4 | 61 | 0.28 | 0.73 | 14 | empty |
| 5 | 57 | 0.26 | 0.73 | 16 | 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 A0LSV2
- Elsewhere: UniProt A0LSV2 · AlphaFold DB A0LSV2
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