Research workbench
Neurotoxin (TS1) from brazilian scorpion tityus serrulatus
Analyse Neurotoxin (TS1) from brazilian scorpion tityus serrulatus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1B7D
- Type
- protein
- Length
- 61 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (neurotoxin TS1)
- UniProt
- P15226
- Ligands
- PO4
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (neurotoxin TS1) | protein | 61 | 13% helix, 25% strand | P15226 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
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 P15226
- Elsewhere: RCSB PDB 1B7D · PDBe 1B7D · UniProt P15226
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