1vj1

Protein Summary

Structure of putative NADPH-dependent oxidoreductase (GI:18204011; COG2130; Pfam00107) from Mouse comprises two distinct domains: the catalytic domain (residues 1-132; 311-351) and the nucleotide-binding domain (residues 133-310). Structure of the catalytic domain has GroES-like fold (SCOP sunid:50128) and  belongs to alcohol dehydrogenase-like family (SCOP sunid:50136). The nucleotide-binding domain has NAD(P)-binding Rossmann-fold domains (SCOP sunid:51734; 3 layers - a/b/a, where parallel beta-sheet of 6 strands has order 321456).

Structural comparison with quinone oxidoreductase, shows that the large cleft between the two domains in GI:18204011 could easily accommodate an NADPH molecule and suggests a redox mechanism related to that of quinone oxidoreductase (PubMed:15229897).