5uc8: Difference between revisions

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 ==Crystal structure of human Heme Oxygenase-2==
-<StructureSection load='5uc8' size='340' side='right' caption='[[5uc8]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='5uc8' size='340' side='right'caption='[[5uc8]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5uc8]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UC8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UC8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5uc8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UC8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UC8 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uc9|5uc9]], [[5uca|5uca]]</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&#8491;</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_(biliverdin-producing) Heme oxygenase (biliverdin-producing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.18 1.14.14.18] </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=5uc8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uc8 OCA], [https://pdbe.org/5uc8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uc8 RCSB], [https://www.ebi.ac.uk/pdbsum/5uc8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uc8 ProSAT]</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=5uc8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uc8 OCA], [http://pdbe.org/5uc8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uc8 RCSB], [http://www.ebi.ac.uk/pdbsum/5uc8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uc8 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HMOX2_HUMAN HMOX2_HUMAN]] 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. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter.
+[https://www.uniprot.org/uniprot/HMOX2_HUMAN HMOX2_HUMAN] 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. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 19: / Line 18: @@
 </div>
 <div class="pdbe-citations 5uc8" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Heme oxygenase 3D structures|Heme oxygenase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Luo, S]]
+[[Category: Homo sapiens]]
-[[Category: Tong, L]]
+[[Category: Large Structures]]
-[[Category: Heme oxygenase]]
+[[Category: Luo S]]
-[[Category: Oxidoreductase]]
+[[Category: Tong L]]