1yb5

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Current revision

Crystal structure of human Zeta-Crystallin with bound NADP

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@@ Line 3: / Line 3: @@
 <StructureSection load='1yb5' size='340' side='right'caption='[[1yb5]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1yb5]] is a 2 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=1YB5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1YB5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1yb5]] is a 2 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=1YB5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YB5 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</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 HUMAN])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='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 id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yb5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yb5 OCA], [https://pdbe.org/1yb5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yb5 RCSB], [https://www.ebi.ac.uk/pdbsum/1yb5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yb5 ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1yb5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yb5 OCA], [http://pdbe.org/1yb5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yb5 RCSB], [http://www.ebi.ac.uk/pdbsum/1yb5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1yb5 ProSAT]</span></td></tr>
 </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>
+[https://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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 23: / Line 22: @@
 ==See Also==
-*[[Quinone reductase|Quinone reductase]]
+*[[Quinone reductase 3D structures|Quinone reductase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[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: Edwards A]]
-[[Category: Delft, F von]]
+[[Category: Gileadi O]]
-[[Category: Edwards, A]]
+[[Category: Kavanagh K]]
-[[Category: Gileadi, O]]
+[[Category: Oppermann U]]
-[[Category: Kavanagh, K]]
+[[Category: Sundstrom M]]
-[[Category: Oppermann, U]]
+[[Category: Williams L]]
-[[Category: Structural genomic]]
+[[Category: Von Delft F]]
-[[Category: Sundstrom, M]]
-[[Category: Williams, L]]
-[[Category: Medium-chain dehydrogenase/reductase]]
-[[Category: Oxidoreductase]]
-[[Category: Quinone reduction]]
-[[Category: Sgc]]

1yb5

From Proteopedia

Current revision

Crystal structure of human Zeta-Crystallin with bound NADP

Structural highlights

Function

Evolutionary Conservation

See Also

References

Contents

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