Literature summary for 3.4.21.53 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.

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Crystallization (Commentary)

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

Protein Variants

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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	-	Archaeoglobus fulgidus

Organism

Organism	UniProt	Comment	Textmining
Archaeoglobus fulgidus	O29883	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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)