Research workbench
Clostridium botulinum type E catalytic domain E212Q mutant
Analyse Clostridium botulinum type E catalytic domain E212Q mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1T3C
- Type
- protein
- Length
- 820 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Neurotoxin type E
- EC
- 3.4.24.69
- UniProt
- Q00496
- Ligands
- ZN, CL
- Pockets
- 6 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Neurotoxin type E (EC 3.4.24.69) | protein | 411 | 35% helix, 17% strand | Q00496 |
| B | Neurotoxin type E (EC 3.4.24.69) | protein | 409 | 36% helix, 18% 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 | 1063 | 0.82 | 0.83 | 106 | empty |
| 2 | 384 | 0.63 | 0.78 | 41 | ZN |
| 3 | 367 | 0.62 | 0.78 | 41 | empty |
| 4 | 94 | 0.36 | 0.74 | 15 | empty |
| 5 | 58 | 0.35 | 0.78 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1296 Ų buried · 12 hydrogen bonds · protein-protein
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 Q00496
- Elsewhere: RCSB PDB 1T3C · PDBe 1T3C · UniProt Q00496
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