Literature summary for 3.4.21.108 extracted from

Merski, M.; Moreira, C.; Abreu, R.M.; Ramos, M.J.; Fernandes, P.A.; Martins, L.M.; Pereira, P.J.B.; Macedo-Ribeiro, S.
Molecular motion regulates the activity of the mitochondrial serine protease HtrA2 (2017), Cell Death Dis., 8, e3119 .

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Crystallization (Commentary)

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

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

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

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	-	Homo sapiens	5739	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O43464	-	-

Synonyms

Synonyms	Comment	Organism
HtrA2	-	Homo sapiens

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
97.3	-	melting temperature	Homo sapiens

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Release 2026.1 (March 2026)