Research workbench
AlphaFold monomer V2.0 prediction for thermal hysteresis protein yl-1 (O16119)
Analyse AlphaFold monomer V2.0 prediction for thermal hysteresis protein yl-1 (O16119) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O16119
- Type
- protein
- Length
- 112 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x16bAB96c6aDA76E246D4ba74AE1dCaf6B052cC5a
- UniProt
- O16119
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 112 | — | O16119 |
Compared structures
- 1EZG · Crystal structure of antifreeze protein from the beetle, tenebrio molitor · an experimental structure of the same protein · chain A against B, TM-score 0.73
- 1EZG · Crystal structure of antifreeze protein from the beetle, tenebrio molitor · an experimental structure of the same protein · chain A against B, TM-score 0.73
- 1L1I · Solution Structure of the Tenebrio molitor Antifreeze Protein · an experimental structure of the same protein · chain A against A, TM-score 0.62
- 1L1I · Solution structure of the tenebrio molitor antifreeze protein · an experimental structure of the same protein · chain A against A, TM-score 0.62
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 O16119
- Elsewhere: UniProt O16119 · AlphaFold DB O16119
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