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1dir
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==CRYSTAL STRUCTURE OF A MONOCLINIC FORM OF DIHYDROPTERIDINE REDUCTASE FROM RAT LIVER== | ==CRYSTAL STRUCTURE OF A MONOCLINIC FORM OF DIHYDROPTERIDINE REDUCTASE FROM RAT LIVER== | ||
| - | <StructureSection load='1dir' size='340' side='right' caption='[[1dir]], [[Resolution|resolution]] 2.60Å' scene=''> | + | <StructureSection load='1dir' size='340' side='right'caption='[[1dir]], [[Resolution|resolution]] 2.60Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1dir]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1dir]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DIR FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dir OCA], [https://pdbe.org/1dir PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dir RCSB], [https://www.ebi.ac.uk/pdbsum/1dir PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dir ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/DHPR_RAT DHPR_RAT] The product of this enzyme, tetrahydrobiopterin (BH-4), is an essential cofactor for phenylalanine, tyrosine, and tryptophan hydroxylases. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/di/1dir_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/di/1dir_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> | ||
| - | </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/ | + | </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=1dir ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | A binary complex of dihydropteridine reductase and NADH crystallizes in the space group C2, with a = 222.2, b = 46.5, c = 95.3 A and beta = 101.1 degrees. There are two dimers in the asymmetric unit. The structure was solved by molecular-replacement techniques and refined with 2.6 A data to a crystallographic R factor of 16.8%. Each dimer has twofold non-crystallographic symmetry and the four individual monomers in the asymmetric unit have the same overall molecular conformation. | ||
| - | |||
| - | Crystal structure of a monoclinic form of dihydropteridine reductase from rat liver.,Su Y, Skinner MM, Xuong NH, Matthews DA, Whiteley JM, Varughese KI Acta Crystallogr D Biol Crystallogr. 1994 Nov 1;50(Pt 6):884-8. PMID:15299357<ref>PMID:15299357</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Matthews | + | [[Category: Matthews DA]] |
| - | [[Category: Skinner | + | [[Category: Skinner MM]] |
| - | [[Category: Su | + | [[Category: Su Y]] |
| - | [[Category: Varughese | + | [[Category: Varughese KI]] |
| - | [[Category: Whitely | + | [[Category: Whitely JM]] |
| - | [[Category: Xuong | + | [[Category: Xuong NH]] |
Current revision
CRYSTAL STRUCTURE OF A MONOCLINIC FORM OF DIHYDROPTERIDINE REDUCTASE FROM RAT LIVER
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