Research workbench
Cryo-EM structure of aerolysin pore in lmng micelle
Analyse Cryo-EM structure of aerolysin pore in lmng micelle in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5JZT
- Type
- protein
- Length
- 2,961 residues
- Chains
- 7
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aerolysin
- UniProt
- P09167
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 1 distinct chain · 16% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | Aerolysin | protein | 423 | 16% helix, 34% strand | P09167 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 639 | 0.86 | 0.90 | 109 | empty |
| 2 | 1053 | 0.82 | 0.83 | 123 | empty |
| 3 | 287 | 0.78 | 0.90 | 57 | empty |
| 4 | 244 | 0.77 | 0.90 | 36 | empty |
| 5 | 316 | 0.77 | 0.88 | 57 | empty |
Interfaces
14 interfaces between chains.
- D–E · 3506 Ų buried · 92 hydrogen bonds · protein-protein
- C–D · 3503 Ų buried · 82 hydrogen bonds · protein-protein
- E–F · 3434 Ų buried · 77 hydrogen bonds · protein-protein
- F–G · 3294 Ų buried · 72 hydrogen bonds · protein-protein
- B–C · 3280 Ų buried · 68 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 P09167
- Elsewhere: RCSB PDB 5JZT · PDBe 5JZT · UniProt P09167
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