4xyj
From Proteopedia
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| - | ''' | + | ==Crystal structure of human phosphofructokinase-1 in complex with ATP and Mg, Northeast Structural Genomics Consortium Target HR9275== |
| - | + | <StructureSection load='4xyj' size='340' side='right' caption='[[4xyj]], [[Resolution|resolution]] 3.10Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4xyj]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XYJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XYJ FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |
| - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xyk|4xyk]]</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> | |
| - | [[Category: | + | <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=4xyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xyj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xyj RCSB], [http://www.ebi.ac.uk/pdbsum/4xyj PDBsum]</span></td></tr> |
| - | [[Category: | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PFKAP_HUMAN PFKAP_HUMAN]] Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: 6-phosphofructokinase]] | ||
| + | [[Category: Barber, D L]] | ||
[[Category: Forouhar, F]] | [[Category: Forouhar, F]] | ||
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | + | ||
| - | + | ||
[[Category: Seetharaman, J]] | [[Category: Seetharaman, J]] | ||
| + | [[Category: Szu, F E]] | ||
| + | [[Category: Tong, L]] | ||
| + | [[Category: Webb, B A]] | ||
| + | [[Category: Nesg]] | ||
| + | [[Category: PSI, Protein structure initiative]] | ||
| + | [[Category: Psi-biology]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 12:19, 20 May 2015
Crystal structure of human phosphofructokinase-1 in complex with ATP and Mg, Northeast Structural Genomics Consortium Target HR9275
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