3wt2: Difference between revisions

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==Crystal structure of the b'-a' domain of thermophilic fungal protein disulfide isomerase (oxidized form)==
==Crystal structure of the b'-a' domain of thermophilic fungal protein disulfide isomerase (oxidized form)==
<StructureSection load='3wt2' size='340' side='right' caption='[[3wt2]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
<StructureSection load='3wt2' size='340' side='right'caption='[[3wt2]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3wt2]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_16454 Atcc 16454]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WT2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WT2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3wt2]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Humicola_insolens Humicola insolens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WT2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WT2 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2kp1|2kp1]], [[2kp2|2kp2]], [[3wt1|3wt1]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3wt2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wt2 OCA], [https://pdbe.org/3wt2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wt2 RCSB], [https://www.ebi.ac.uk/pdbsum/3wt2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wt2 ProSAT]</span></td></tr>
<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=3wt2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wt2 OCA], [http://pdbe.org/3wt2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wt2 RCSB], [http://www.ebi.ac.uk/pdbsum/3wt2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wt2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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).  
[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).
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 16454]]
[[Category: Humicola insolens]]
[[Category: Protein disulfide-isomerase]]
[[Category: Large Structures]]
[[Category: Inagaki, K]]
[[Category: Inagaki K]]
[[Category: Itoh, S G]]
[[Category: Itoh SG]]
[[Category: Kato, K]]
[[Category: Kato K]]
[[Category: Okumura, H]]
[[Category: Okumura H]]
[[Category: Satoh, T]]
[[Category: Satoh T]]
[[Category: Disulfide bond]]
[[Category: Endoplasmic reticulum]]
[[Category: Isomerase]]
[[Category: Oxidoreductase]]
[[Category: Thioredoxin]]
[[Category: Thioredoxin fold]]