1umk

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==The Structure of Human Erythrocyte NADH-cytochrome b5 Reductase==
==The Structure of Human Erythrocyte NADH-cytochrome b5 Reductase==
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<StructureSection load='1umk' size='340' side='right' caption='[[1umk]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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<StructureSection load='1umk' size='340' side='right'caption='[[1umk]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1umk]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UMK FirstGlance]. <br>
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<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>
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</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>
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</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>
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<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>
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<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>
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<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://www.rcsb.org/pdb/explore.do?structureId=1umk RCSB], [http://www.ebi.ac.uk/pdbsum/1umk PDBsum]</span></td></tr>
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<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>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/NCB5R_HUMAN NCB5R_HUMAN]] Defects in CYB5R3 are the cause of methemoglobinemia CYB5R3-related (METHB-CYB5R3) [MIM:[http://omim.org/entry/250800 250800]]. A form of methemoglobinemia, a hematologic disease characterized by the presence of excessive amounts of methemoglobin in blood cells, resulting in decreased oxygen carrying capacity of the blood, cyanosis and hypoxia. There are two types of methemoglobinemia CYB5R3-related. In type 1, the defect affects the soluble form of the enzyme, is restricted to red blood cells, and causes well-tolerated methemoglobinemia. In type 2, the defect affects both the soluble and microsomal forms of the enzyme and is thus generalized, affecting red cells, leukocytes and all body tissues. Type 2 methemoglobinemia is associated with mental deficiency and other neurologic symptoms.<ref>PMID:1898726</ref> <ref>PMID:1707593</ref> <ref>PMID:1400360</ref> <ref>PMID:8119939</ref> <ref>PMID:7718898</ref> <ref>PMID:9695975</ref> <ref>PMID:9886302</ref> <ref>PMID:10807796</ref> <ref>PMID:15622768</ref> <ref>PMID:12393396</ref> <ref>PMID:15953014</ref>
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[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 ==
== Function ==
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[[http://www.uniprot.org/uniprot/NCB5R_HUMAN NCB5R_HUMAN]] Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction.
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[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/um/1umk_consurf.spt"</scriptWhenChecked>
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<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>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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</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].
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</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="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 1umk" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[NADH-cytochrome b5 reductase|NADH-cytochrome b5 reductase]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cytochrome-b5 reductase]]
 
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Bando, S]]
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[[Category: Large Structures]]
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[[Category: Horii, C]]
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[[Category: Bando S]]
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[[Category: Nakagawa, A]]
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[[Category: Horii C]]
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[[Category: Shirabe, K]]
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[[Category: Nakagawa A]]
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[[Category: Takano, T]]
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[[Category: Shirabe K]]
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[[Category: Takeshita, M]]
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[[Category: Takano T]]
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[[Category: Yubisui, T]]
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[[Category: Takeshita M]]
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[[Category: Beta barrel]]
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[[Category: Yubisui T]]
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[[Category: Fad-binding domain]]
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[[Category: Flavoprotein]]
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[[Category: Nadh-binding domain]]
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[[Category: Oxidoreductase]]
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Current revision

The Structure of Human Erythrocyte NADH-cytochrome b5 Reductase

PDB ID 1umk

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