Research workbench
NMR solution structure for shk-192: a potent KV1.3-specific immunosuppressive polypeptide
Analyse NMR solution structure for shk-192: a potent KV1.3-specific immunosuppressive… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2K9E
- Type
- protein
- Length
- 36 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Potassium channel toxin shk
- UniProt
- P29187
- Ligands
- NH2
Structure
solution nmr · 1 distinct chain · 39% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Potassium channel toxin shk | protein | 36 | 39% helix, 0% strand | P29187 |
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, 2 modified (disulfide, nonstandard).
Compared structures
- 2K9E · NMR Solution Structure for ShK-192: A Potent KV1.3-Specific Immunosuppressive Polypeptide · the same entry in another collection · chain A against A, TM-score 1.00
- P29187 · AlphaFold monomer V2.0 prediction for kappa-stichotoxin-SHE3A (P29187) · a predicted model of the same protein · chain A against A, TM-score 0.70
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 P29187
- Elsewhere: RCSB PDB 2K9E · PDBe 2K9E · UniProt P29187
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