2djj
From Proteopedia
(Difference between revisions)
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<StructureSection load='2djj' size='340' side='right'caption='[[2djj]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | <StructureSection load='2djj' size='340' side='right'caption='[[2djj]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2djj]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2djj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_16454 Atcc 16454]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1xtx 1xtx]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DJJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DJJ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2djk|2djk]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2djk|2djk]]</div></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2djj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2djj OCA], [https://pdbe.org/2djj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2djj RCSB], [https://www.ebi.ac.uk/pdbsum/2djj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2djj ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/PDI_HUMIN PDI_HUMIN]] Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer (By similarity). |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 10:32, 8 December 2021
Solution structure of the a' domain of thermophilic fungal protein disulfide isomerase
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