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AlphaFold monomer V2.0 prediction for ATP-dependent protease subunit hslv (A3PG34)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent protease subunit hslv… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A3PG34
- Type
- protein
- Length
- 185 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x03eE9dF280950A2b9f9DE96506c6093Adc158ac7
- UniProt
- A3PG34
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 185 | — | A3PG34 |
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 A3PG34
- Elsewhere: UniProt A3PG34 · AlphaFold DB A3PG34
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