Research workbench
Cryoem structure of the membrane pore complex of pneumolysin at 4.5A
Analyse Cryoem structure of the membrane pore complex of pneumolysin at 4.5A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LY6
- Type
- protein
- Length
- 471 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pneumolysin
- UniProt
- Q04IN8
- Pockets
- 6 · best druggability 0.68
Structure
electron microscopy · 1 distinct chain · 13% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Pneumolysin | protein | 471 | 13% helix, 36% strand | Q04IN8 |
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 | 89 | 0.68 | 0.92 | 21 | empty |
| 2 | 156 | 0.61 | 0.84 | 30 | empty |
| 3 | 170 | 0.55 | 0.80 | 31 | empty |
| 4 | 60 | 0.44 | 0.82 | 19 | empty |
| 5 | 83 | 0.42 | 0.80 | 17 | 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 Q04IN8
- Elsewhere: RCSB PDB 5LY6 · PDBe 5LY6 · UniProt Q04IN8
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