| Primary Identifier | IPR023210 | Type | Domain |
| Short Name | NADP_OxRdtase_dom |
| description | The aldo-keto reductase family includes a number of related monomeric NADPH-dependent oxidoreductases, such as aldehyde reductase, aldose reductase, prostaglandin F synthase, xylose reductase, rho crystallin, and many others []. All possess a similar structure, with a beta-α-β fold characteristic of nucleotide binding proteins []. The fold comprises a parallel beta-8/alpha-8-barrel, which contains a novel NADP-binding motif. The binding site is located in a large,deep, elliptical pocket in the C-terminal end of the beta sheet, the substrate being bound in an extended conformation. The hydrophobicnature of the pocket favours aromatic and apolar substrates over highly polar ones [].Binding of the NADPH coenzyme causes a massive conformational change, reorienting a loop, effectively locking thecoenzyme in place. This binding is more similar to FAD- than to NAD(P)-binding oxidoreductases [].Some proteins of this entry contain a K+ ion channel beta chain regulatory domain; these are reported to have oxidoreductase activity []. This entry represents the NADP-dependent oxidoreductase domain found in these proteins. |
