1vm6
From Proteopedia
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- | {{Seed}} | ||
- | [[Image:1vm6.png|left|200px]] | ||
- | + | ==Crystal structure of Dihydrodipicolinate reductase (TM1520) from Thermotoga maritima at 2.27 A resolution== | |
- | + | <StructureSection load='1vm6' size='340' side='right'caption='[[1vm6]], [[Resolution|resolution]] 2.27Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[1vm6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VM6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VM6 FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.27Å</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></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=1vm6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vm6 OCA], [https://pdbe.org/1vm6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vm6 RCSB], [https://www.ebi.ac.uk/pdbsum/1vm6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vm6 ProSAT], [https://www.topsan.org/Proteins/JCSG/1vm6 TOPSAN]</span></td></tr> | |
- | + | </table> | |
- | + | == Function == | |
- | + | [https://www.uniprot.org/uniprot/DAPB_THEMA DAPB_THEMA] Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate (Probable). Uses NADPH as a reductant with much more efficiency than NADH.<ref>PMID:18250105</ref> | |
- | + | == Evolutionary Conservation == | |
- | == | + | [[Image:Consurf_key_small.gif|200px|right]] |
- | + | Check<jmol> | |
- | [[Category: | + | <jmolCheckbox> |
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vm/1vm6_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/main_output.php?pdb_ID=1vm6 ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
- | [[Category: JCSG, Joint Center for Structural Genomics.]] | ||
- | [[Category: Dihydrodipicolinate reductase]] | ||
- | [[Category: Jcsg]] | ||
- | [[Category: Joint center for structural genomic]] | ||
- | [[Category: Protein structure initiative]] | ||
- | [[Category: Psi]] | ||
- | [[Category: Structural genomic]] | ||
- | [[Category: Tm1520]] | ||
- | |||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Nov 16 17:56:36 2008'' |
Current revision
Crystal structure of Dihydrodipicolinate reductase (TM1520) from Thermotoga maritima at 2.27 A resolution
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