Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent clp protease proteolytic subunit (Q5SKM8)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent clp protease proteolytic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5SKM8
- Type
- protein
- Length
- 194 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x114a0357b11cFf6EBe7075749Ec3390CD780d178
- UniProt
- Q5SKM8
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 194 | — | Q5SKM8 |
Compared structures
- 6HWM · Structure of Thermus thermophilus ClpP in complex with bortezomib · an experimental structure of the same protein · chain A against E, TM-score 0.95
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 Q5SKM8
- Elsewhere: UniProt Q5SKM8 · AlphaFold DB Q5SKM8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.