Literature summary for 3.1.21.3 extracted from

Obarska-Kosinska, A.; Taylor, J.E.; Callow, P.; Orlowski, J.; Bujnicki, J.M.; Kneale, G.G.
HsdR subunit of the type I restriction-modification enzyme EcoR124I: biophysical characterisation and structural modelling (2008), J. Mol. Biol., 376, 438-452.

Search for more literature for 3.1.21.3

Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
model of subunit HsdR using protein fold-recognition and homology modeling. Subunit shows an ellipsoidal shape of the enzymatic core comprising the N-terminal and central domains. Conformational heterogenity of the C-terminal region implicated in binding of HsdR to the HsdS-HsdM complex	Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
94000	-	1 * 94000, dynamic light scattering, 1 * 130000, analytical ultracentrifugation, subunit HsdR, subunit is globular and fairly compact	Escherichia coli
130000	-	1 * 94000, dynamic light scattering, 1 * 130000, analytical ultracentrifugation, subunit HsdR, subunit is globular and fairly compact	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	Q304R3	HsdR subunit of isoform EcoR124I	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Subunits

Subunits	Comment	Organism
monomer	1 * 94000, dynamic light scattering, 1 * 130000, analytical ultracentrifugation, subunit HsdR, subunit is globular and fairly compact	Escherichia coli

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)