1a33: Difference between revisions

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 <StructureSection load='1a33' size='340' side='right'caption='[[1a33]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1a33]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bruma Bruma]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A33 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1A33 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1a33]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brugia_malayi Brugia malayi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A33 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A33 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BMCYP-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6279 BRUMA])</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]] 2.15&#8491;</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'>[https://proteopedia.org/fgij/fg.htm?mol=1a33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a33 OCA], [https://pdbe.org/1a33 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a33 RCSB], [https://www.ebi.ac.uk/pdbsum/1a33 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a33 ProSAT]</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=1a33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a33 OCA], [http://pdbe.org/1a33 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a33 RCSB], [http://www.ebi.ac.uk/pdbsum/1a33 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1a33 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CYP1_BRUMA CYP1_BRUMA]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
+[https://www.uniprot.org/uniprot/CYP1_BRUMA CYP1_BRUMA] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Bruma]]
+[[Category: Brugia malayi]]
 [[Category: Large Structures]]
-[[Category: Peptidylprolyl isomerase]]
+[[Category: Carlow CKS]]
-[[Category: Carlow, C K.S]]
+[[Category: Ma D]]
-[[Category: Ma, D]]
+[[Category: Mikol V]]
-[[Category: Mikol, V]]
-[[Category: Isomerase]]
-[[Category: Peptidyl-prolyl cis-tran]]

1a33: Difference between revisions

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