Research workbench
Analysis of side-chain organization on a refined model of charybdotoxin: structural and functional implications
Analyse Analysis of side-chain organization on a refined model of charybdotoxin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CRD
- Type
- protein
- Length
- 37 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Charybdotoxin
- UniProt
- P13487
Structure
solution nmr · 1 distinct chain · 27% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Charybdotoxin | protein | 37 | 27% helix, 19% strand | P13487 |
Modifications
Observed in the structure: 3 disulfide, 1 modified (disulfide, cyclization).
Compared structures
- 2CRD · Analysis of side-chain organization on a refined model of charybdotoxin: structural and… · the same entry in another collection · chain A against A, TM-score 1.00
- P13487 · AlphaFold monomer V2.0 prediction for potassium channel toxin alpha- ktx 1.1 (P13487) · 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 P13487
- Elsewhere: RCSB PDB 2CRD · PDBe 2CRD · UniProt P13487
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