View source for 9med


==Crystal Structure Pyrophosphate-fructose 6-phosphate 1-phosphotransferase 1 (Pfk1) from Trichomonas vaginalis (AMP/beta-D-Glucose-6-phosphate complex)==
<StructureSection load='9med' size='340' side='right'caption='[[9med]], [[Resolution|resolution]] 2.62&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9med]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichomonas_vaginalis_G3 Trichomonas vaginalis G3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9MED OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9MED 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]] 2.62&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=BG6:BETA-D-GLUCOSE-6-PHOSPHATE'>BG6</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=PPV:PYROPHOSPHATE'>PPV</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=9med FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9med OCA], [https://pdbe.org/9med PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9med RCSB], [https://www.ebi.ac.uk/pdbsum/9med PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9med ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PFP1_TRIV3 PFP1_TRIV3] 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_01979]<ref>PMID:2558319</ref> 
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Trichomonas vaginalis G3]]
[[Category: Structural genomic]]