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1ok4
From Proteopedia
(Difference between revisions)
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<StructureSection load='1ok4' size='340' side='right'caption='[[1ok4]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1ok4' size='340' side='right'caption='[[1ok4]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1ok4]] is a 10 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1ok4]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35583 Atcc 35583]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OK4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OK4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=13P:1,3-DIHYDROXYACETONEPHOSPHATE'>13P</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=13P:1,3-DIHYDROXYACETONEPHOSPHATE'>13P</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ojx|1ojx]], [[1ok6|1ok6]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ojx|1ojx]], [[1ok6|1ok6]]</div></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ok4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ok4 OCA], [https://pdbe.org/1ok4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ok4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ok4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ok4 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/ALF1_THETK ALF1_THETK]] Catalyzes the reversible cleavage of fructose 1,6-bisphosphate (FBP) to glyceraldehyde 3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP). |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 06:01, 28 April 2021
Archaeal fructose 1,6-bisphosphate aldolase covalently bound to the substrate dihydroxyacetone phosphate
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Categories: Atcc 35583 | Fructose-bisphosphate aldolase | Large Structures | Hensel, R | Lorentzen, E | Pohl, E | Siebers, B | Stark, A | Zwart, P | 6-bisphosphate | Aldolase | Archaeal | Fructose 1 | Glycolytic | Lyase | Tim barrel

