Crystallization (Comment) | Organism |
---|---|
to 1.65 A resolution. The catalytic triad in the HtrA2 wild-type structure is disrupted, with the nearest accessible H198 side chain atom positioned 5.9 A away from the carboxylate oxygen of D228 and separated from the hydroxyl of S306 by 7.4 A, requiring substantial rearrangements to reestablish a catalytically competent conformation. Dynamic protein motions are important to HtrA protease activity | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
S306A | presence of a serine residue in position 306 favors an inactive conformation of H198, thereby perturbing the geometry of the active site | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | - |
Homo sapiens | 5739 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | O43464 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
HtrA2 | - |
Homo sapiens |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
97.3 | - |
melting temperature | Homo sapiens |