1irm: Difference between revisions

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 <StructureSection load='1irm' size='340' side='right'caption='[[1irm]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1irm]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IRM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IRM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1irm]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IRM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IRM FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qq8|1qq8]], [[1dve|1dve]], [[1dvg|1dvg]], [[1j77|1j77]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qq8|1qq8]], [[1dve|1dve]], [[1dvg|1dvg]], [[1j77|1j77]]</div></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </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=1irm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1irm OCA], [http://pdbe.org/1irm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1irm RCSB], [http://www.ebi.ac.uk/pdbsum/1irm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1irm 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=1irm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1irm OCA], [https://pdbe.org/1irm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1irm RCSB], [https://www.ebi.ac.uk/pdbsum/1irm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1irm ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HMOX1_RAT HMOX1_RAT]] Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed.
+[[https://www.uniprot.org/uniprot/HMOX1_RAT HMOX1_RAT]] Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]