Sandbox6 Eric Martz: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
Eric Martz (talk | contribs)
No edit summary
Eric Martz (talk | contribs)
Line 21: Line 21:
* This model shows a <scene name='Sandbox6_Eric_Martz/2-88_charge/1'>noteworthy separation of charges</scene>, with a large region containing only negative charges.
* This model shows a <scene name='Sandbox6_Eric_Martz/2-88_charge/1'>noteworthy separation of charges</scene>, with a large region containing only negative charges.
<center>{{Template:ColorKey_Charge_Anionic}} / {{Template:ColorKey_Charge_Cationic}}</center>
<center>{{Template:ColorKey_Charge_Anionic}} / {{Template:ColorKey_Charge_Cationic}}</center>
*I am still working on the analysis of evolutionary conservation in this model. (I ran into some problem with the ConSurf server and am communicating with the group in Tel-Aviv.)
*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 <scene name='Sandbox6_Eric_Martz/2-88_conservation/1'>conserved patch</scene> 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.)
**Cartoon
**Cartoon decorated with conserved residues
**<scene name='Sandbox6_Eric_Martz/2-88_conservation/1'>Spacefilling</scene>
*This model can be downloaded from [[:Image:Caspase12-homology-model-2-88-on-1dgn-a.pdb|model-2-88]].
*This model can be downloaded from [[:Image:Caspase12-homology-model-2-88-on-1dgn-a.pdb|model-2-88]].


===Notes===
===Notes===
<references />
<references />

Revision as of 23:33, 9 February 2011

Please do not edit this page. Eric Martz, February 2011.

Homology Model for 83-341Homology Model for 83-341

Drag the structure with the mouse to rotate
  • 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. .

Homology Model for 2-88Homology Model for 2-88

  • 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.)
    • Cartoon
    • Cartoon decorated with conserved residues
  • This model can be downloaded from model-2-88.

NotesNotes

  1. ConSurf run using 80 sequences from the Uniref-90 sequence database. MSA average pairwise distance (APD) 0.94.

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Eric Martz