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AlphaFold monomer V2.0 prediction for ATP-dependent clp protease ATP- binding subunit clpx (B0VKU4)
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
- B0VKU4
- Type
- protein
- Length
- 437 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9823334B175F9f2683922fd5F25c4D9e96Fd15E9
- Molecule
- ATP-dependent clp protease ATP-binding subunit clpx
- UniProt
- B0VKU4
- Pockets
- 4 · best druggability 0.59
Structure
1 distinct chain · 42% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent clp protease ATP-binding subunit clpx | protein | 437 | 42% helix, 13% strand | B0VKU4 |
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 | 284 | 0.59 | 0.78 | 31 | empty |
| 2 | 146 | 0.46 | 0.76 | 20 | empty |
| 3 | 90 | 0.39 | 0.77 | 21 | empty |
| 4 | 69 | 0.31 | 0.74 | 22 | 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 B0VKU4
- Elsewhere: UniProt B0VKU4 · AlphaFold DB B0VKU4
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