Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent clp protease ATP- binding subunit clpx (Q6D826)
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
- Q6D826
- Type
- protein
- Length
- 424 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3E00F62D3140A99ec52E6a60794edd4CcC68D67b
- Molecule
- ATP-dependent clp protease ATP-binding subunit clpx
- UniProt
- Q6D826
- Pockets
- 4 · best druggability 0.59
Structure
1 distinct chain · 43% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent clp protease ATP-binding subunit clpx | protein | 424 | 43% helix, 15% strand | Q6D826 |
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 | 264 | 0.59 | 0.79 | 31 | empty |
| 2 | 140 | 0.43 | 0.75 | 17 | empty |
| 3 | 72 | 0.38 | 0.78 | 20 | empty |
| 4 | 51 | 0.30 | 0.76 | 15 | 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 Q6D826
- Elsewhere: UniProt Q6D826 · AlphaFold DB Q6D826
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