Research workbench
Determination of the three-dimensional structure of scyllatoxin by 1H nuclear magnetic resonance
Analyse Determination of the three-dimensional structure of scyllatoxin by 1H nuclear… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SCY
- Type
- protein
- Length
- 31 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Scyllatoxin
- UniProt
- P16341
- Ligands
- NH2
Structure
solution nmr · 1 distinct chain · 32% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Scyllatoxin | protein | 31 | 32% helix, 26% strand | P16341 |
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.
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1SCY · Determination of the three-dimensional structure of scyllatoxin by 1H nuclear magnetic… · the same entry in another collection · chain A against A, TM-score 1.00
- P16341 · AlphaFold monomer V2.0 prediction for potassium channel toxin alpha- ktx 5.1 (P16341) · a predicted model of the same protein · chain A against A, TM-score 0.78
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 P16341
- Elsewhere: RCSB PDB 1SCY · PDBe 1SCY · UniProt P16341
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