6o6i
From Proteopedia
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==Endoplasmic reticulum protein 29 (ERp29) C-terminal domain: Structure Determination from Backbone Amide Pseudocontact Shifts Generated by Double-histidine Cobalt Tags== | ==Endoplasmic reticulum protein 29 (ERp29) C-terminal domain: Structure Determination from Backbone Amide Pseudocontact Shifts Generated by Double-histidine Cobalt Tags== | ||
| - | <StructureSection load='6o6i' size='340' side='right'caption='[[6o6i | + | <StructureSection load='6o6i' size='340' side='right'caption='[[6o6i]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6o6i]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O6I OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6o6i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O6I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O6I FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6o6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o6i OCA], [https://pdbe.org/6o6i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o6i RCSB], [https://www.ebi.ac.uk/pdbsum/6o6i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o6i ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/ERP29_RAT ERP29_RAT] Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER. |
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| - | + | ==See Also== | |
| - | + | *[[ER-resident protein|ER-resident protein]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Rattus norvegicus]] |
| - | [[Category: | + | [[Category: Bahramzadeh A]] |
| - | [[Category: | + | [[Category: Huber T]] |
| - | [[Category: | + | [[Category: Otting G]] |
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Current revision
Endoplasmic reticulum protein 29 (ERp29) C-terminal domain: Structure Determination from Backbone Amide Pseudocontact Shifts Generated by Double-histidine Cobalt Tags
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