v5.1.0.3
Glycine data from LIS
Type | Domain |
Description | SelM and Sep15 consists of one catalytic a-domain that assumes a thioredoxin-like fold composed of a mixed four-stranded β-sheet and three interspersed α-helices. The active-site redox motifs of SelM and Sep15 are located between the C terminus of strand beta1 and the N terminus of helix alpha1. SelM and Sep15 may function as thiol-disulphide isomerases involved in disulphide bond formation in the endoplasmic reticulum [ ]. |
Short Name | Sep15_SelM_dom |