Literature summary for 2.1.1.321 extracted from

Cura, V.; Troffer-Charlier, N.; Wurtz, J.M.; Bonnefond, L.; Cavarelli, J.
Structural insight into arginine methylation by the mouse protein arginine methyltransferase 7: a zinc finger freezes the mimic of the dimeric state into a single active site (2014), Acta Crystallogr. Sect. D, 70, 2401-2412.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Mus musculus

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of full-length PRMT7 at 1.7 A resolution. The PRMT7 structure is composed of two catalytic modules in tandem forming a pseudo-dimer and contains only one AdoHcy molecule bound to the N-terminal module. The second active site is frozen in an inactive state by a conserved zinc finger located at the junction between the two PRMT modules and by the collapse of two degenerated AdoMet-binding loops	Mus musculus

Crystallization (Comment)

Organism

crystal structure of full-length PRMT7 at 1.7 A resolution. The PRMT7 structure is composed of two catalytic modules in tandem forming a pseudo-dimer and contains only one AdoHcy molecule bound to the N-terminal module. The second active site is frozen in an inactive state by a conserved zinc finger located at the junction between the two PRMT modules and by the collapse of two degenerated AdoMet-binding loops

Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q922X9	isoform PRMT7	-

Synonyms

Synonyms	Comment	Organism
PRMT7	-	Mus musculus

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Release 2023.1 (January 2023)