5j6e: Difference between revisions

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OCA

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 ==Structure of disulfide crosslinked A. fumigatus FKBP12(V91C)==
-<StructureSection load='5j6e' size='340' side='right' caption='[[5j6e]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
+<StructureSection load='5j6e' size='340' side='right'caption='[[5j6e]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5j6e]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J6E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J6E FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5j6e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus_Af293 Aspergillus fumigatus Af293]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J6E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5J6E FirstGlance]. <br>
-</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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</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=5j6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j6e OCA], [http://pdbe.org/5j6e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j6e RCSB], [http://www.ebi.ac.uk/pdbsum/5j6e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j6e ProSAT]</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=5j6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j6e OCA], [https://pdbe.org/5j6e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5j6e RCSB], [https://www.ebi.ac.uk/pdbsum/5j6e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5j6e ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FKB1A_ASPFU FKB1A_ASPFU]] 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/FKB1A_ASPFU FKB1A_ASPFU] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
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 ==See Also==
-*[[FK506 binding protein|FK506 binding protein]]
+*[[FKBP 3D structures|FKBP 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Peptidylprolyl isomerase]]
+[[Category: Aspergillus fumigatus Af293]]
-[[Category: Schumacher, M]]
+[[Category: Large Structures]]
-[[Category: Crosslinked dimer]]
+[[Category: Schumacher M]]
-[[Category: Disulfide trapping]]
-[[Category: Fkbp12]]
-[[Category: Isomerase]]