Literature summary for 3.1.31.1 extracted from

Leung, K.W.; Liaw, Y.C.; Chan, S.C.; Lo, H.Y.; Musayev, F.N.; Chen, J.Z.; Fang, H.J.; Chen, H.M.
Significance of local electrostatic interactions in staphylococcal nuclease studied by site-directed mutagenesis (2001), J. Biol. Chem., 276, 46039-46045.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapor diffusion method	Staphylococcus sp.

Protein Variants

Protein Variants	Comment	Organism
D77G	loss of catalytic efficiency of 16% and thermal stabilty of 26% relative to the wild-type protein	Staphylococcus sp.
E73G	loss of catalytic efficiency of 24% and thermal stabilty of 22% relative to the wild-type protein	Staphylococcus sp.
E73G/D77G	loss of thermal stabilty of 47% relative to the wild-type protein	Staphylococcus sp.
E73G/E75G	loss of thermal stabilty of 59% relative to the wild-type protein	Staphylococcus sp.
E73G/E75G/D77G	loss of thermal stabilty of 65% relative to the wild-type protein	Staphylococcus sp.
E75G/D77G	loss of thermal stabilty of 58% relative to the wild-type protein	Staphylococcus sp.

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus sp.	-	-	-

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Release 2023.1 (January 2023)