Homology model of 83-341 on template chain A of 3e4c, 52% sequence identity (). Confidence in this model is high because of the 52% sequence identity and sequence alignment with only one 10-residue gap.
Amino Terminus
Carboxy Terminus
.
The seems unremarkable. Bear in mind that sidechain rotamer positions are incorrect in a homology model.
Anionic (-) / Cationic (+)
The inner face of 95-140 is . Bear in mind that sidechain rotamer positions are incorrect in a homology model. . The distribution of hydrophobic residues in 83-140 of the homology model is similar to that in the .
The inner face of 95-140 is , even based upon a multiple sequence alignment that includes mostly types other than 12[1] .
When the multiple sequence alignment is limited to the 14 type-12 sequences available from Uniprot (APD 0.30), most of the residues have insufficient data, but a , namely Asn130, Val135, Val136, Glu139, Asn140. .
Swiss-Model produced a using chain A of 1dgn as template. Confidence in this model is low because the sequence alignment had only 19% identity.
This model shows a , with a large region containing only negative charges.
Anionic (-) / Cationic (+)
Analysis of evolutionary conservation for 2-88 is difficult because not enough related sequences are available in Uniprot. Thus most of the residues have "insufficient data" (yellow). Despite the paucity of information, there appears to be a that may be of interest. (To identify the conserved residues, toggle spinning off, then touch each residue with the mouse, and observe the popup "hover" report.)
