2djk

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<StructureSection load='2djk' size='340' side='right'caption='[[2djk]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
<StructureSection load='2djk' size='340' side='right'caption='[[2djk]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2djk]] is a 1 chain structure with sequence from [http://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=1v52 1v52]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DJK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DJK FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2djk]] 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=1v52 1v52]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DJK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DJK FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2djj|2djj]]</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;'>[[2djj|2djj]]</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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2djk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2djk OCA], [http://pdbe.org/2djk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2djk RCSB], [http://www.ebi.ac.uk/pdbsum/2djk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2djk 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=2djk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2djk OCA], [https://pdbe.org/2djk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2djk RCSB], [https://www.ebi.ac.uk/pdbsum/2djk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2djk 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).
== 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 b' domain of thermophilic fungal protein disulfide isomerase

PDB ID 2djk

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