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1fea
From Proteopedia
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==UNLIGANDED CRITHIDIA FASCICULATA TRYPANOTHIONE REDUCTASE AT 2.2 ANGSTROM RESOLUTION== | ==UNLIGANDED CRITHIDIA FASCICULATA TRYPANOTHIONE REDUCTASE AT 2.2 ANGSTROM RESOLUTION== | ||
| - | <StructureSection load='1fea' size='340' side='right' caption='[[1fea]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='1fea' size='340' side='right'caption='[[1fea]], [[Resolution|resolution]] 2.20Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1fea]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1fea]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Crithidia_fasciculata Crithidia fasciculata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FEA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FEA FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | |
| - | <tr id=' | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fea OCA], [https://pdbe.org/1fea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fea RCSB], [https://www.ebi.ac.uk/pdbsum/1fea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fea ProSAT]</span></td></tr> |
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/TYTR_CRIFA TYTR_CRIFA] Trypanothione is the parasite analog of glutathione; this enzyme is the equivalent of glutathione reductase. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fe/1fea_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fe/1fea_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| - | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fea ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Crithidia fasciculata]] | [[Category: Crithidia fasciculata]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Karplus | + | [[Category: Karplus P]] |
| - | [[Category: Strickland | + | [[Category: Strickland C]] |
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Current revision
UNLIGANDED CRITHIDIA FASCICULATA TRYPANOTHIONE REDUCTASE AT 2.2 ANGSTROM RESOLUTION
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