Research workbench
AlphaFold monomer V2.0 prediction for lipoprotein signal peptidase (Q9HVM5)
Analyse AlphaFold monomer V2.0 prediction for lipoprotein signal peptidase (Q9HVM5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9HVM5
- Type
- protein
- Length
- 169 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd10960F956646DE8b64d3598984c91C2d5Af3D7b
- UniProt
- Q9HVM5
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 169 | — | Q9HVM5 |
Compared structures
- 5DIR · membrane protein at 2.8 Angstroms · an experimental structure of the same protein · chain A against A, TM-score 0.87
- 5DIR · Membrane protein at 2.8 ångströms · an experimental structure of the same protein · chain A against A, TM-score 0.87
- 6FMS · Imisx-ep of se-lspa · an experimental structure of the same protein · chain A against A, TM-score 0.86
- 6FMS · IMISX-EP of Se-LspA · an experimental structure of the same protein · chain A against A, TM-score 0.86
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 Q9HVM5
- Elsewhere: UniProt Q9HVM5 · AlphaFold DB Q9HVM5
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