Research workbench
Solution Structure of HERG Specific Scorpion Toxin CnErg1
Analyse Solution Structure of HERG Specific Scorpion Toxin CnErg1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NE5
- Type
- protein
- Length
- 42 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- NOT
- Molecule
- ergtoxin
- UniProt
- Q86QT3
Structure
solution nmr · resolution NOT · 1 distinct chain · 31% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ergtoxin | protein | 42 | 31% helix, 21% strand | Q86QT3 |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1NE5 · Solution structure of herg specific scorpion toxin CNERG1 · the same entry in another collection · chain A against A, TM-score 1.00
- Q86QT3 · AlphaFold monomer V2.0 prediction for potassium channel toxin gamma- ktx 1.1 (Q86QT3) · a predicted model of the same protein · chain A against A, TM-score 0.72
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 Q86QT3
- Elsewhere: RCSB PDB 1NE5 · PDBe 1NE5 · UniProt Q86QT3
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