6qu3: Difference between revisions
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==Crystal Structure of Phosphofructokinase from Trypanosoma brucei in complex with an allosteric inhibitor ctcb360== | |||
<StructureSection load='6qu3' size='340' side='right'caption='[[6qu3]], [[Resolution|resolution]] 2.35Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6qu3]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QU3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QU3 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=JJ5:1-[(3,4-dichlorophenyl)methyl]-7~{H}-pyrrolo[3,2-c]pyridin-4-one'>JJ5</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr> | |||
[[Category: | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3f5m|3f5m]], [[2hig|2hig]]</td></tr> | ||
[[Category: | <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6qu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qu3 OCA], [http://pdbe.org/6qu3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qu3 RCSB], [http://www.ebi.ac.uk/pdbsum/6qu3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qu3 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/PFKA_TRYBB PFKA_TRYBB]] Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.[HAMAP-Rule:MF_03186] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: 6-phosphofructokinase]] | |||
[[Category: Large Structures]] | |||
[[Category: Dornan, J]] | [[Category: Dornan, J]] | ||
[[Category: Walkinshaw, M | [[Category: McNae, I W]] | ||
[[Category: Walkinshaw, M D]] | |||
[[Category: Allostery]] | |||
[[Category: Glycolysis]] | |||
[[Category: Inhibitor]] | |||
[[Category: Transferase]] | |||
Revision as of 09:48, 18 March 2020
Crystal Structure of Phosphofructokinase from Trypanosoma brucei in complex with an allosteric inhibitor ctcb360
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