3k2q: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 3k2q is ON HOLD
+==Crystal structure of Pyrophosphate-dependent phosphofructokinase from Marinobacter aquaeolei, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET MqR88==
+<StructureSection load='3k2q' size='340' side='right'caption='[[3k2q]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3k2q]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Marinobacter_nauticus_VT8 Marinobacter nauticus VT8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K2Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K2Q 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]] 2.5&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=3k2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k2q OCA], [https://pdbe.org/3k2q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k2q RCSB], [https://www.ebi.ac.uk/pdbsum/3k2q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k2q ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/A1U3A9_MARN8 A1U3A9_MARN8] Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.[HAMAP-Rule:MF_01978]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k2/3k2q_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=3k2q ConSurf].
+<div style="clear:both"></div>
-Authors: J. Seetharaman, H. Neely, Sahdev, S. , Janjua, H. , Xiao, R. , Ciccosanti, C. , Foote, E.L , Acton, T.B., Rost, B. , Montelione, G.T. , Tong, L. , Hunt, J.F, Northeast Structural Genomics Consortium (NESG)
+==See Also==
+*[[Phosphofructokinase 3D structures|Phosphofructokinase 3D structures]]
-Description: Crystal structure of Pyrophosphate-dependent phosphofructokinase from Marinobacter aquaeolei, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET MqR88
+__TOC__
+</StructureSection>
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct  7 13:45:26 2009''
+[[Category: Large Structures]]
+[[Category: Marinobacter nauticus VT8]]
+[[Category: Acton TB]]
+[[Category: Baran MC]]
+[[Category: Cunningham K]]
+[[Category: Hunt JF]]
+[[Category: Janjua K]]
+[[Category: Lew S]]
+[[Category: Liu J]]
+[[Category: Montelione GT]]
+[[Category: Neely H]]
+[[Category: Owens L]]
+[[Category: Rost B]]
+[[Category: Seetharaman J]]
+[[Category: Tong L]]
+[[Category: Wang D]]
+[[Category: Xiao R]]