Literature summary for 5.3.4.1 extracted from

Tian, G.; Kober, F.X.; Lewandrowski, U.; Sickmann, A.; Lennarz, W.J.; Schindelin, H.
The catalytic activity of protein-disulfide isomerase requires a conformationally flexible molecule (2008), J. Biol. Chem., 283, 33630-33640.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
to 3.7 A resolution. PDI is a highly flexible molecule with its catalytic domains, a and a', representing two mobile arms connected to a more rigid core composed of the b and b' domains. The linker between the a domain and the core is more susceptible to degradation than that connecting the a' domain to the core. Molecular flexibility is essential for the enzymatic activity in vitro and in vivo	Saccharomyces cerevisiae

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
endoplasmic reticulum	enzyme exists as an interconvertible mixture of monomers and dimers	Saccharomyces cerevisiae	5783	-

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Subunits

Subunits	Comment	Organism
dimer	crystallization data	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)