4omt: Difference between revisions

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 ==Crystal structure of human muscle phosphofructokinase (dissociated homodimer)==
-<StructureSection load='4omt' size='340' side='right' caption='[[4omt]], [[Resolution|resolution]] 6.00&Aring;' scene=''>
+<StructureSection load='4omt' size='340' side='right'caption='[[4omt]], [[Resolution|resolution]] 6.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4omt]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OMT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OMT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4omt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OMT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OMT FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3o8n|3o8n]], [[3opy|3opy]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 6&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/6-phosphofructokinase 6-phosphofructokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.11 2.7.1.11] </span></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=4omt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4omt OCA], [https://pdbe.org/4omt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4omt RCSB], [https://www.ebi.ac.uk/pdbsum/4omt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4omt ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4omt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4omt OCA], [http://pdbe.org/4omt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4omt RCSB], [http://www.ebi.ac.uk/pdbsum/4omt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4omt ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/K6PF_HUMAN K6PF_HUMAN]] Glycogen storage disease due to muscle phosphofructokinase deficiency. The disease is caused by mutations affecting the gene represented in this entry.
+[https://www.uniprot.org/uniprot/PFKAM_HUMAN PFKAM_HUMAN] Glycogen storage disease due to muscle phosphofructokinase deficiency. The disease is caused by variants affecting the gene represented in this entry.
 == Function ==
-[[http://www.uniprot.org/uniprot/K6PF_HUMAN K6PF_HUMAN]] Catalyzes the third step of glycolysis, the phosphorylation of fructose-6-phosphate (F6P) by ATP to generate fructose-1,6-bisphosphate (FBP) and ADP.[HAMAP-Rule:MF_00339]
+[https://www.uniprot.org/uniprot/PFKAM_HUMAN PFKAM_HUMAN] Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
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 ==See Also==
-*[[Phosphofructokinase (PFK)|Phosphofructokinase (PFK)]]
+*[[Phosphofructokinase 3D structures|Phosphofructokinase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: 6-phosphofructokinase]]
+[[Category: Homo sapiens]]
-[[Category: Kloos, M]]
+[[Category: Large Structures]]
-[[Category: Straeter, N]]
+[[Category: Kloos M]]
-[[Category: 6-phosphofructokinase activity]]
+[[Category: Straeter N]]
-[[Category: Fructose 6-phosphate]]
-[[Category: Human 6-phosphofructokinase]]
-[[Category: Transferase]]