Literature summary extracted from
Deswarte, J.; De Vos, S.; Langhorst, U.; Steyaert, J.; Loris, R.
The contribution of metal ions to the conformational stability of ribonuclease T1: crystal versus solution (2001), Eur. J. Biochem., 268, 3993-4000.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
4.6.1.24 |
two crystal forms obtained, the classic crystal form I, and the crystals of form II, obtained by repeated seeding |
Aspergillus oryzae |
General Stability
EC Number |
General Stability |
Organism |
---|
4.6.1.24 |
the enzyme is remarkably stable at high salt concentrations |
Aspergillus oryzae |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
4.6.1.24 |
Ca2+ |
the enzyme has six binding sites for the cation |
Aspergillus oryzae |
|
4.6.1.24 |
Sr2+ |
the enzyme contains a divalent ion-binding site involving Asp49, with preference for this cation. The ion binding at this site stabilizes the protein |
Aspergillus oryzae |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.6.1.24 |
Aspergillus oryzae |
- |
- |
- |