Comparison of predicted sequence and structure features between wild-type and mutant XPA protein. Secondary structure is depicted as green (alpha-helices) and orange (beta-sheets) boxes. Prediction of coiled coil regions is shown as grey bar. Red diamonds indicate cysteins involved in disulfide bonds, whereas dashed connections show predicted bonds between them. Blue boxes indicate regions of functional domains determined by Interpro and Prosite. Prosite Pattern: PS_1: Protein kinase C phosphorylation site, PS_2: XPA protein signature 1, PS_3: XPA protein signature 2, PS_4: Casein kinase II phosphorylation site, PS_5: cAMP- and cGMP-dependent protein kinase phosphorylation site, PS_6: N-myristoylation site. Interpro-Domains: IPR_1: DNA binding domain, putative, IPR_2: Zinc finger, XPA-type, conserved site, IPR_3: XPA-type C-terminal, IPR_4: XPA conserved site.