Literature summary extracted from

Botos, I.; Melnikov, E.E.; Cherry, S.; Kozlov, S.; Makhovskaya, O.V.; Tropea, J.E.; Gustchina, A.; Rotanova, T.V.; Wlodawer, A.
Atomic-resolution crystal structure of the proteolytic domain of Archaeoglobus fulgidus lon reveals the conformational variability in the active sites of lon proteases (2005), J. Mol. Biol., 351, 144-157.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
3.4.21.53	proteolytic domain, residues 415-621, and comparison with mutants D508A, S509A, E506A	Archaeoglobus fulgidus

Protein Variants

EC Number	Protein Variants	Comment	Organism
3.4.21.53	D508A	reduction of enzymic activity	Archaeoglobus fulgidus
3.4.21.53	E506A	reduction of enzymic activity	Archaeoglobus fulgidus
3.4.21.53	S509A	loss of enzymic activity	Archaeoglobus fulgidus

Metals/Ions

EC Number	Metals/Ions	Comment	Organism	Structure
3.4.21.53	Ca2+	-	Archaeoglobus fulgidus

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.4.21.53	Archaeoglobus fulgidus	O29883	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3.4.21.53	additional information	wild-type shows considerable ATP-dependent activity when assayed at 70°C	Archaeoglobus fulgidus	?	-	?

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Release 2023.1 (January 2023)