Research workbench
Crystal structure of Arg347Ala mutant of botulinum neurotoxin E catalytic domain
Analyse Crystal structure of Arg347Ala mutant of botulinum neurotoxin E catalytic domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZKW
- Type
- protein
- Length
- 820 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.17
- Source
- Clostridium botulinum
- Molecule
- botulinum neurotoxin type E
- EC
- 3.4.24.69
- UniProt
- Q00496
- Ligands
- ZN, CL
- Pockets
- 6 · best druggability 0.81
Structure
x-ray diffraction · resolution 2.17 · 2 distinct chains · 35% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | botulinum neurotoxin type E (EC 3.4.24.69) | protein | 411 | 35% helix, 18% strand | Q00496 |
| B | botulinum neurotoxin type E (EC 3.4.24.69) | protein | 409 | 35% helix, 17% strand | Q00496 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1095 | 0.81 | 0.82 | 108 | empty |
| 2 | 416 | 0.66 | 0.79 | 49 | empty |
| 3 | 389 | 0.64 | 0.78 | 52 | CL |
| 4 | 69 | 0.34 | 0.76 | 24 | empty |
| 5 | 87 | 0.33 | 0.74 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1263 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 1ZKW · Crystal structure of ARG347ALA mutant of botulinum neurotoxin E catalytic domain · the same entry in another collection · chain A against A, TM-score 1.00
- Q00496 · AlphaFold monomer V2.0 prediction for botulinum neurotoxin type E (Q00496) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 Q00496
- Elsewhere: RCSB PDB 1ZKW · PDBe 1ZKW · UniProt Q00496
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