5ht1: Difference between revisions

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<StructureSection load='5ht1' size='340' side='right'caption='[[5ht1]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
<StructureSection load='5ht1' size='340' side='right'caption='[[5ht1]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5ht1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Canga Canga]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HT1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5HT1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5ht1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_glabrata_CBS_138 Candida glabrata CBS 138]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HT1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HT1 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hua|5hua]]</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]] 2.651&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FPR1, CAGL0K09724g ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284593 CANGA])</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=5ht1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ht1 OCA], [https://pdbe.org/5ht1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ht1 RCSB], [https://www.ebi.ac.uk/pdbsum/5ht1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ht1 ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ht1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ht1 OCA], [http://pdbe.org/5ht1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ht1 RCSB], [http://www.ebi.ac.uk/pdbsum/5ht1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ht1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/FKBP_CANGA FKBP_CANGA]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).  
[https://www.uniprot.org/uniprot/FKBP_CANGA FKBP_CANGA] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
*[[FK506 binding protein|FK506 binding protein]]
*[[FKBP 3D structures|FKBP 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Canga]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Schumacher MA]]
[[Category: Schumacher, M A]]
[[Category: C. glabrata]]
[[Category: Fkbp12]]
[[Category: Isomerase]]
[[Category: Pahtogenesis]]

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