Research workbench
TRICHOTOXIN_A50E, an ion channel-forming polypeptide
Analyse TRICHOTOXIN_A50E, an ion channel-forming polypeptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1M24
- Type
- protein
- Length
- 34 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TRICHOTOXIN_A50E
- Ligands
- ACE, VOL, CCN
Structure
x-ray diffraction · 1 distinct chain · 88% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | TRICHOTOXIN_A50E | protein | 17 | 88% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · 2 copies · chains A, B
- VOL · L-valinol · ligand · 2 copies · chains A, B
- CCN · Acetonitrile · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 228 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 18 modified, 4 covalent (nonstandard, covalent ligand).
Compared structures
- 1M24 · Trichotoxin_A50E, An Ion Channel-Forming Polypeptide · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 1M24 · PDBe 1M24
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