Research workbench
NMR and restrained molecular dynamics study of the three-dimensional solution structure of toxin FS2, a specific blocker of the L-type calcium channel, isolated from black mamba venom
Analyse NMR and restrained molecular dynamics study of the three-dimensional solution… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TFS
- Type
- protein
- Length
- 60 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Toxin FS2
- UniProt
- P01414
Structure
solution nmr · 1 distinct chain · 0% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Toxin FS2 | protein | 60 | 0% helix, 50% strand | P01414 |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1TFS · NMR and restrained molecular dynamics study of the three-dimensional solution structure… · the same entry in another collection · chain A against A, TM-score 1.00
- P01414 · AlphaFold monomer V2.0 prediction for toxin fs-2 (P01414) · a predicted model of the same protein · chain A against A, TM-score 0.80
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 P01414
- Elsewhere: RCSB PDB 1TFS · PDBe 1TFS · UniProt P01414
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