1umk: Difference between revisions

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OCA

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 ==The Structure of Human Erythrocyte NADH-cytochrome b5 Reductase==
-<StructureSection load='1umk' size='340' side='right' caption='[[1umk]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
+<StructureSection load='1umk' size='340' side='right'caption='[[1umk]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1umk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UMK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UMK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1umk]] is a 1 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=1UMK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UMK FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></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]] 1.75&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cytochrome-b5_reductase Cytochrome-b5 reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.2.2 1.6.2.2] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></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=1umk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1umk OCA], [http://pdbe.org/1umk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1umk RCSB], [http://www.ebi.ac.uk/pdbsum/1umk PDBsum]</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=1umk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1umk OCA], [https://pdbe.org/1umk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1umk RCSB], [https://www.ebi.ac.uk/pdbsum/1umk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1umk ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/NB5R3_HUMAN NB5R3_HUMAN]] Recessive hereditary methemoglobinemia type 2;Recessive hereditary methemoglobinemia type 1. The disease is caused by mutations affecting the gene represented in this entry.
+[https://www.uniprot.org/uniprot/NB5R3_HUMAN NB5R3_HUMAN] Recessive hereditary methemoglobinemia type 2;Recessive hereditary methemoglobinemia type 1. The disease is caused by mutations affecting the gene represented in this entry.
 == Function ==
-[[http://www.uniprot.org/uniprot/NB5R3_HUMAN NB5R3_HUMAN]] Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction.
+[https://www.uniprot.org/uniprot/NB5R3_HUMAN NB5R3_HUMAN] Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/um/1umk_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/um/1umk_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1umk ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 30: / Line 31: @@
 </div>
 <div class="pdbe-citations 1umk" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[NADH-cytochrome b5 reductase|NADH-cytochrome b5 reductase]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Cytochrome-b5 reductase]]
+[[Category: Homo sapiens]]
-[[Category: Human]]
+[[Category: Large Structures]]
-[[Category: Bando, S]]
+[[Category: Bando S]]
-[[Category: Horii, C]]
+[[Category: Horii C]]
-[[Category: Nakagawa, A]]
+[[Category: Nakagawa A]]
-[[Category: Shirabe, K]]
+[[Category: Shirabe K]]
-[[Category: Takano, T]]
+[[Category: Takano T]]
-[[Category: Takeshita, M]]
+[[Category: Takeshita M]]
-[[Category: Yubisui, T]]
+[[Category: Yubisui T]]
-[[Category: Beta barrel]]
-[[Category: Fad-binding domain]]
-[[Category: Flavoprotein]]
-[[Category: Nadh-binding domain]]
-[[Category: Oxidoreductase]]