9mdt
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure Pyrophosphate-fructose 6-phosphate 1-phosphotransferase 1 (Pfk1) from Trichomonas vaginalis (ATP/Pyrophosphate complex)== | |
| - | + | <StructureSection load='9mdt' size='340' side='right'caption='[[9mdt]], [[Resolution|resolution]] 2.16Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[9mdt]] 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=9MDT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9MDT 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]] 2.16Å</td></tr> | |
| - | [[Category: | + | <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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=PPV:PYROPHOSPHATE'>PPV</scene></td></tr> |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9mdt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9mdt OCA], [https://pdbe.org/9mdt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9mdt RCSB], [https://www.ebi.ac.uk/pdbsum/9mdt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9mdt 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/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Trichomonas vaginalis G3]] | ||
| + | [[Category: Structural genomic]] | ||
Current revision
Crystal Structure Pyrophosphate-fructose 6-phosphate 1-phosphotransferase 1 (Pfk1) from Trichomonas vaginalis (ATP/Pyrophosphate complex)
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