1QJH
Protein Aggregation and Alzheimer's Disease: Crystallographic Analysis of the Phenomenon. Engineered version of the ribosomal protein S6 used as a stable scaffold to study oligomerization.
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | 30S ribosomal protein S6 | polymer | 101 | 11830.7 | 1 | UniProt (P23370) Pfam (PF01250) | Thermus thermophilus | TS9 |
| 2 | B (A) | MAGNESIUM ION | non-polymer | 24.3 | 1 | Chemie (MG) | |||
| 3 | C (A) | water | water | 18.0 | 45 | Chemie (HOH) |
Sequence modifications
A: 1 - 101 (UniProt: P23370)
| PDB | External Database | Details |
|---|---|---|
| Ala 41 | Glu 41 | engineered mutation |
| Ile 42 | Glu 42 | engineered mutation |
| Met 46 | Arg 46 | engineered mutation |
| Val 47 | Arg 47 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 11830.7 | |
| Non-Polymers* | Number of molecules | 1 |
| Total formula weight | 24.3 | |
| All* | Total formula weight | 11855.0 |
