Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent clp protease ATP- binding subunit clpx (B0SEC2)
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
- B0SEC2
- Type
- protein
- Length
- 426 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d3Bd79Ba2ACACeE4ea169Badb24A7837154dEcf
- Molecule
- ATP-dependent clp protease ATP-binding subunit clpx
- UniProt
- B0SEC2
- Pockets
- 4 · best druggability 0.58
Structure
1 distinct chain · 43% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent clp protease ATP-binding subunit clpx | protein | 426 | 43% helix, 14% strand | B0SEC2 |
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 | 223 | 0.58 | 0.79 | 32 | empty |
| 2 | 54 | 0.36 | 0.79 | 15 | empty |
| 3 | 54 | 0.30 | 0.75 | 15 | empty |
| 4 | 53 | 0.29 | 0.76 | 14 | 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 B0SEC2
- Elsewhere: UniProt B0SEC2 · AlphaFold DB B0SEC2
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