Research workbench
The clavanin peptide in the presence of tfe (2,2,2-trifluoroethanol), presented a amphipathic alpha-helices from phe-2 to val-22 residues
Analyse The clavanin peptide in the presence of tfe (2,2,2-trifluoroethanol), presented… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6C41
- Type
- protein
- Length
- 23 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Clavanin-a
- UniProt
- P80710
- Ligands
- NH2
Structure
solution nmr · 1 distinct chain · 91% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Clavanin-a | protein | 23 | 91% helix, 0% strand | P80710 |
Ligands and binding sites
- NH2 · Amino group · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6C41 · The clavanin peptide in the presence of TFE (2,2,2-trifluoroethanol), presented a… · the same entry in another collection · chain A against A, TM-score 1.00
- P80710 · AlphaFold monomer V2.0 prediction for clavanin-a (P80710) · a predicted model of the same protein · chain A against A, TM-score 0.39
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 P80710
- Elsewhere: RCSB PDB 6C41 · PDBe 6C41 · UniProt P80710
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