Research workbench
Crystal structure of the botulinum neurotoxin serotype G binding domain
Analyse Crystal structure of the botulinum neurotoxin serotype G binding domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VXR
- Type
- protein
- Length
- 428 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Botulinum neurotoxin type G
- UniProt
- Q60393
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Botulinum neurotoxin type G | protein | 428 | 7% helix, 45% strand | Q60393 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 172 | 0.55 | 0.80 | 24 | empty |
| 2 | 89 | 0.49 | 0.82 | 24 | empty |
| 3 | 91 | 0.32 | 0.73 | 19 | empty |
Compared structures
- 2VXR · Crystal Structure of the Botulinum Neurotoxin serotype G binding domain · the same entry in another collection · chain A against A, TM-score 1.00
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 Q60393
- Elsewhere: RCSB PDB 2VXR · PDBe 2VXR · UniProt Q60393
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