Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent protease subunit hslv (B7LA29)
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
- B7LA29
- Type
- protein
- Length
- 176 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8A32Ab8cb45a0317B7188057FD938cCf172efEFA
- UniProt
- B7LA29
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 176 | — | B7LA29 |
Compared structures
- 5JI3 · HslUV complex · an experimental structure of the same protein · chain A against D, TM-score 0.97
- 5JI3 · Hsluv complex · an experimental structure of the same protein · chain A against A, TM-score 0.97
- 5JI2 · Hslu L199Q in hsluv complex · an experimental structure of the same protein · chain A against A, TM-score 0.97
- 5JI2 · HslU L199Q in HslUV complex · an experimental structure of the same protein · chain A against A, TM-score 0.97
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 B7LA29
- Elsewhere: UniProt B7LA29 · AlphaFold DB B7LA29
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