Research workbench
AlphaFold monomer V2.0 prediction for humanin (Q8IVG9)
Analyse AlphaFold monomer V2.0 prediction for humanin (Q8IVG9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8IVG9
- Type
- protein
- Length
- 24 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0EA189b2343A464f560b44103f6A3396Da1dA8a9
- UniProt
- Q8IVG9
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 24 | — | Q8IVG9 |
Compared structures
- 1Y32 · NMR structure of humanin in 30% TFE solution · an experimental structure of the same protein · chain A against A, TM-score 0.40
- 1Y32 · NMR structure of humanin in 30% tfe solution · an experimental structure of the same protein · chain A against A, TM-score 0.40
- 2GD3 · NMR structure of S14G-humanin in 30% TFE solution · an experimental structure of the same protein · chain A against A, TM-score 0.38
- 2GD3 · NMR structure of S14G-humanin in 30% tfe solution · an experimental structure of the same protein · chain A against A, TM-score 0.38
- 5GIW · Solution NMR structure of Humanin containing a D-isomerized serine residue · an experimental structure of the same protein · chain A against X, TM-score 0.27
- 5GIW · Solution NMR structure of humanin containing a D-isomerized serine residue · an experimental structure of the same protein · chain A against X, TM-score 0.27
- 7WVX · Cryo-EM structure of the human formyl peptide receptor 2 in complex with fhumanin and Gi2 · an experimental structure of the same protein · chain A against L, TM-score 0.18
- 7WVX · Cryo-EM structure of the human formyl peptide receptor 2 in complex with fhumanin and GI2 · an experimental structure of the same protein · chain A against L, TM-score 0.18
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 Q8IVG9
- Elsewhere: UniProt Q8IVG9 · AlphaFold DB Q8IVG9
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