Literature summary extracted from

Sica, F.; Di Fiore, A.; Merlino, A.; Mazzarella, L.
Structure and stability of the non-covalent swapped dimer of bovine seminal ribonuclease: an enzyme tailored to evade ribonuclease protein inhibitor (2004), J. Biol. Chem., 279, 36753-36760.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
4.6.1.18	crystallization in presence of 2'-deoxycitidylyl(3'-5')-2'-deoxyadenosine at 4°C by using sitting drop vapor diffusion method. Crystal structure of the MxM isomer of the enzyme in the non-covalent dimer form, carboxyamidomethylated at residues Cys31 and Cys32, in a complex with 2'-deoxycitidylyl(3'-5')-2'-deoxyadenosine	Bos taurus

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
4.6.1.18	ribonuclease protein inhibitor	the native enzyme is an equilibrium mixture of two isomers, MxM and M=M. In the former the two subunits swap their N-terminal helices. In the reducing environment of the cytosol, isoform M=M dissociates into monomers, which are strongly inhibited by ribonuclease protein inhibitor, wheras isoform MxM remains as a non-covalent dimer which evades ribonuclease protein inhibitor	Bos taurus

Organism

EC Number	Organism	UniProt	Comment	Textmining
4.6.1.18	Bos taurus	-	-	-

Subunits

EC Number	Subunits	Comment	Organism
4.6.1.18	dimer	BS-RNase is covalent dimer with two intersubunit disulfide bridges between Cys31 of one chain and Cys32 of the second and vice versa. The native enzyme is an equilibrium mixture of two isomers, MxM and M=M. In the former the two subunits swap their N-terminal helices. In the reducing environment of cytosol, M=M dissociates into monomers, which are strongly inhibited by ribonuclease protein inhibitor, wheras MxM remains as a non-covalent dimer which evades ribonuclease protein inhibitor	Bos taurus

Synonyms

EC Number	Synonyms	Comment	Organism
4.6.1.18	BS-RNase	-	Bos taurus
4.6.1.18	seminal ribonuclease	-	Bos taurus

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Release 2023.1 (January 2023)