Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent clp protease ATP- binding subunit clpx (B2GGB7)
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
- B2GGB7
- Type
- protein
- Length
- 431 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0787bC904B7be1a8Bd84a0CF1b68B9B4567D88eb
- Molecule
- ATP-dependent clp protease ATP-binding subunit clpx
- UniProt
- B2GGB7
- Pockets
- 4 · best druggability 0.58
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 | B2GGB7 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 200 | 0.58 | 0.80 | 24 | empty |
| 2 | 236 | 0.52 | 0.76 | 22 | empty |
| 3 | 97 | 0.46 | 0.80 | 19 | empty |
| 4 | 87 | 0.31 | 0.73 | 17 | 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 B2GGB7
- Elsewhere: UniProt B2GGB7 · AlphaFold DB B2GGB7
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