1yb5
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1yb5]] is a 2 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=1YB5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YB5 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1yb5]] is a 2 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=1YB5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YB5 FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CRYZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CRYZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NADPH:quinone_reductase NADPH:quinone reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.5.5 1.6.5.5] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NADPH:quinone_reductase NADPH:quinone reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.5.5 1.6.5.5] </span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yb5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yb5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1yb5 RCSB], [http://www.ebi.ac.uk/pdbsum/1yb5 PDBsum]</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=1yb5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yb5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1yb5 RCSB], [http://www.ebi.ac.uk/pdbsum/1yb5 PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/QOR_HUMAN QOR_HUMAN]] Does not have alcohol dehydrogenase activity. Binds NADP and acts through a one-electron transfer process. Orthoquinones, such as 1,2-naphthoquinone or 9,10-phenanthrenequinone, are the best substrates (in vitro). May act in the detoxification of xenobiotics. Interacts with (AU)-rich elements (ARE) in the 3'-UTR of target mRNA species. Enhances the stability of mRNA coding for BCL2. NADPH binding interferes with mRNA binding.<ref>PMID:17497241</ref> <ref>PMID:20103721</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Quinone reductase|Quinone reductase]] | *[[Quinone reductase|Quinone reductase]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: NADPH:quinone reductase]] | [[Category: NADPH:quinone reductase]] | ||
| - | [[Category: Arrowsmith, C | + | [[Category: Arrowsmith, C]] |
| - | [[Category: Berridge, G | + | [[Category: Berridge, G]] |
| - | [[Category: Bray, J | + | [[Category: Bray, J]] |
| - | [[Category: Colbrook, S | + | [[Category: Colbrook, S]] |
| - | [[Category: Debreczeni, J | + | [[Category: Debreczeni, J]] |
| - | [[Category: Delft, F von | + | [[Category: Delft, F von]] |
| - | [[Category: Edwards, A | + | [[Category: Edwards, A]] |
| - | [[Category: Gileadi, O | + | [[Category: Gileadi, O]] |
| - | [[Category: Kavanagh, K | + | [[Category: Kavanagh, K]] |
| - | [[Category: Oppermann, U | + | [[Category: Oppermann, U]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: Sundstrom, M | + | [[Category: Sundstrom, M]] |
| - | [[Category: Williams, L | + | [[Category: Williams, L]] |
[[Category: Medium-chain dehydrogenase/reductase]] | [[Category: Medium-chain dehydrogenase/reductase]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Quinone reduction]] | [[Category: Quinone reduction]] | ||
[[Category: Sgc]] | [[Category: Sgc]] | ||
| - | [[Category: Structural genomic]] | ||
| - | [[Category: Structural genomics consortium]] | ||
Revision as of 09:11, 25 December 2014
Crystal structure of human Zeta-Crystallin with bound NADP
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Categories: Homo sapiens | NADPH:quinone reductase | Arrowsmith, C | Berridge, G | Bray, J | Colbrook, S | Debreczeni, J | Delft, F von | Edwards, A | Gileadi, O | Kavanagh, K | Oppermann, U | Structural genomic | Sundstrom, M | Williams, L | Medium-chain dehydrogenase/reductase | Oxidoreductase | Quinone reduction | Sgc
