4akh

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Current revision (11:29, 20 December 2023) (edit) (undo)
 
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<StructureSection load='4akh' size='340' side='right'caption='[[4akh]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
<StructureSection load='4akh' size='340' side='right'caption='[[4akh]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4akh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Blood_fluke Blood fluke]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AKH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AKH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4akh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [https://en.wikipedia.org/wiki/Schistosoma_japonicum Schistosoma japonicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AKH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AKH FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.6&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1b8x|1b8x]], [[1dug|1dug]], [[1gne|1gne]], [[1gta|1gta]], [[1gtb|1gtb]], [[1m99|1m99]], [[1m9a|1m9a]], [[1m9b|1m9b]], [[1u87|1u87]], [[1u88|1u88]], [[1ua5|1ua5]], [[1y6e|1y6e]], [[4ai6|4ai6]], [[4akg|4akg]], [[4aki|4aki]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4akh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4akh OCA], [https://pdbe.org/4akh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4akh RCSB], [https://www.ebi.ac.uk/pdbsum/4akh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4akh ProSAT]</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=4akh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4akh OCA], [https://pdbe.org/4akh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4akh RCSB], [https://www.ebi.ac.uk/pdbsum/4akh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4akh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/GST26_SCHJA GST26_SCHJA]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.
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[https://www.uniprot.org/uniprot/DYHC_YEAST DYHC_YEAST] Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required to maintain uniform nuclear distribution in hyphae. May play an important role in the proper orientation of the mitotic spindle into the budding daughter cell yeast. Probably required for normal progression of the cell cycle.<ref>PMID:15642746</ref> [https://www.uniprot.org/uniprot/GST26_SCHJA GST26_SCHJA] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Blood fluke]]
 
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[[Category: Glutathione transferase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Carter, A P]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Gleave, E S]]
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[[Category: Schistosoma japonicum]]
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[[Category: Schmidt, H]]
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[[Category: Carter AP]]
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[[Category: Aaa+ protein]]
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[[Category: Gleave ES]]
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[[Category: Asce protein]]
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[[Category: Schmidt H]]
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[[Category: Cytoskeletal motor]]
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[[Category: Motor protein]]
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[[Category: Motor protein p-loop ntpase]]
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[[Category: Motor protein-transferase complex]]
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Current revision

Dynein Motor Domain - AMPPNP complex

PDB ID 4akh

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