Research workbench
Solution structure of the tenebrio molitor antifreeze protein
Analyse Solution structure of the tenebrio molitor antifreeze protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1L1I
- Type
- protein
- Length
- 84 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thermal hysteresis protein isoform yl-1 (2-14)
- UniProt
- O16119
Structure
solution nmr · 1 distinct chain · 0% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thermal hysteresis protein isoform yl-1 (2-14) | protein | 84 | 0% helix, 12% strand | O16119 |
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 1L1I · Solution Structure of the Tenebrio molitor Antifreeze Protein · the same entry in another collection · chain A against A, TM-score 1.00
- O16119 · AlphaFold monomer V2.0 prediction for thermal hysteresis protein yl-1 (O16119) · a predicted model of the same protein · chain A against A, TM-score 0.79
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: RCSB PDB 1L1I · PDBe 1L1I · UniProt O16119
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