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1.3.99.36
dodecamer
a CypD monomer consists of a single classic Rossmann-fold domain, which is composed of a central beta-sheet formed by six parallel strands (labeled beta1-beta6) enclosed by eight alpha helices (labeled alpha1-alpha8). Residues that participate in forming the trimer (trimer contacts) are found in a region spanning alpha5 and alpha6, and a region containing alpha7 and a long loop in the terminus of alpha7, whereas interactions between trimers (dimer contacts) are found mainly within alpha1, and a region spanning alpha2 and alpha3
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763030
1.3.99.36
dodecamer
each monomer consists of a classic Rossmann-fold domain. This domain is constructed by a central beta sheet consisting of six parallel strands, which are enclosed by eight alpha helices. A fragment spanning Asn156-Ala166 is not observed in the CypD structure, which is likely responsible in substrate binding
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763314
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