2rue

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<StructureSection load='2rue' size='340' side='right'caption='[[2rue]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
<StructureSection load='2rue' size='340' side='right'caption='[[2rue]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2rue]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_16454 Atcc 16454]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RUE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2RUE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2rue]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_16454 Atcc 16454]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RUE FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2kp1|2kp1]], [[2kp2|2kp2]]</td></tr>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2kp1|2kp1]], [[2kp2|2kp2]]</div></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] </span></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2rue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rue OCA], [http://pdbe.org/2rue PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rue RCSB], [http://www.ebi.ac.uk/pdbsum/2rue PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rue ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rue OCA], [https://pdbe.org/2rue PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rue RCSB], [https://www.ebi.ac.uk/pdbsum/2rue PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rue ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://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).
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[[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).
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 12:27, 23 March 2022

Solution structure of the a' domain of thermophilic fungal protein disulfide (oxidized form, 303K)

PDB ID 2rue

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