Research workbench
Tetanus neurotoxin mutant-(H233A/E234Q/H237A/Y375F)
Analyse Tetanus neurotoxin mutant-(H233A/E234Q/H237A/Y375F) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BY5
- Type
- protein
- Length
- 1,286 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tetanus toxin
- EC
- 3.4.24.68
- UniProt
- P04958
- Ligands
- NA, CL
- Pockets
- 15 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tetanus toxin (EC 3.4.24.68) | protein | 1286 | 30% helix, 25% strand | P04958 |
Ligands and binding sites
- NA · Sodium ion · metal · 3 copies · chains A
- CL · Chloride ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 8 copies · chains A
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1136 | 0.84 | 0.85 | 80 | EPE |
| 2 | 838 | 0.82 | 0.84 | 90 | NA |
| 3 | 761 | 0.79 | 0.83 | 85 | empty |
| 4 | 266 | 0.70 | 0.85 | 33 | EDO |
| 5 | 273 | 0.62 | 0.80 | 28 | empty |
Modifications
Observed in the structure: 1 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 P04958
- Elsewhere: RCSB PDB 7BY5 · PDBe 7BY5 · UniProt P04958
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