Research workbench
Crystal structure of botulinum neurotoxin type B at pH 5.0
Analyse Crystal structure of botulinum neurotoxin type B at pH 5.0 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1S0C
- Type
- protein
- Length
- 1,287 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Botulinum neurotoxin type B
- EC
- 3.4.24.69
- UniProt
- P10844
- Ligands
- CA, ZN
- Pockets
- 14 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Botulinum neurotoxin type B (EC 3.4.24.69) | protein | 1287 | 32% helix, 24% strand | P10844 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 768 | 0.82 | 0.85 | 103 | empty |
| 2 | 862 | 0.80 | 0.83 | 70 | ZN |
| 3 | 458 | 0.66 | 0.78 | 58 | empty |
| 4 | 60 | 0.64 | 0.94 | 22 | empty |
| 5 | 477 | 0.63 | 0.76 | 39 | empty |
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 P10844
- Elsewhere: RCSB PDB 1S0C · PDBe 1S0C · UniProt P10844
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