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Crystal structure of pneumolysin D168A mutant.
Analyse Crystal structure of pneumolysin D168A mutant. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5AOE
- Type
- protein
- Length
- 976 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pneumolysin
- UniProt
- Q04IN8
- Pockets
- 11 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Pneumolysin | protein | 488 | 18% helix, 40% strand | Q04IN8 |
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 195 | 0.61 | 0.82 | 34 | empty |
| 2 | 211 | 0.60 | 0.81 | 38 | empty |
| 3 | 85 | 0.54 | 0.85 | 22 | empty |
| 4 | 92 | 0.53 | 0.84 | 20 | empty |
| 5 | 125 | 0.51 | 0.80 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 305 Ų buried · 3 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 Q04IN8
- Elsewhere: RCSB PDB 5AOE · PDBe 5AOE · UniProt Q04IN8
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