1x5c
From Proteopedia
(Difference between revisions)
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<StructureSection load='1x5c' size='340' side='right'caption='[[1x5c]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1x5c' size='340' side='right'caption='[[1x5c]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1x5c]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1x5c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X5C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X5C FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">P4HB ([ | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">P4HB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1x5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x5c OCA], [https://pdbe.org/1x5c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x5c RCSB], [https://www.ebi.ac.uk/pdbsum/1x5c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x5c ProSAT], [https://www.topsan.org/Proteins/RSGI/1x5c TOPSAN]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/PDIA1_HUMAN PDIA1_HUMAN]] This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP.<ref>PMID:10636893</ref> <ref>PMID:12485997</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 07:05, 2 March 2022
The solution structure of the second thioredoxin-like domain of human Protein disulfide-isomerase
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Categories: Human | Large Structures | Protein disulfide-isomerase | Inoue, M | Kigawa, T | Koshiba, S | Structural genomic | Tochio, N | Yokoyama, S | Dsi | Erba2l | Git | Isomerase | National project on protein structural and functional analyse | Nppsfa | Pdi | Pdia1 | Po4db | Po4hb | Prohb | Redox | Rsgi | Thioredoxin like domain
