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1typ

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{{STRUCTURE_1typ| PDB=1typ | SCENE= }}
 
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===SUBSTRATE INTERACTIONS BETWEEN TRYPANOTHIONE REDUCTASE AND N1-GLUTATHIONYLSPERMIDINE DISULPHIDE AT 0.28-NM RESOLUTION===
 
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{{ABSTRACT_PUBMED_8477734}}
 
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==About this Structure==
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==SUBSTRATE INTERACTIONS BETWEEN TRYPANOTHIONE REDUCTASE AND N1-GLUTATHIONYLSPERMIDINE DISULPHIDE AT 0.28-NM RESOLUTION==
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[[1typ]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Crithidia_fasciculata Crithidia fasciculata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TYP OCA].
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<StructureSection load='1typ' size='340' side='right'caption='[[1typ]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1typ]] is a 2 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=1TYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TYP FirstGlance]. <br>
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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]] 2.8&#8491;</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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SPD:SPERMIDINE'>SPD</scene></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=1typ FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1typ OCA], [https://pdbe.org/1typ PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1typ RCSB], [https://www.ebi.ac.uk/pdbsum/1typ PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1typ ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TYTR_CRIFA TYTR_CRIFA] Trypanothione is the parasite analog of glutathione; this enzyme is the equivalent of glutathione reductase.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ty/1typ_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1typ ConSurf].
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<div style="clear:both"></div>
==See Also==
==See Also==
*[[Trypanothione reductase|Trypanothione reductase]]
*[[Trypanothione reductase|Trypanothione reductase]]
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__TOC__
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==Reference==
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</StructureSection>
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<ref group="xtra">PMID:008477734</ref><references group="xtra"/>
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[[Category: Crithidia fasciculata]]
[[Category: Crithidia fasciculata]]
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[[Category: Trypanothione-disulfide reductase]]
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[[Category: Large Structures]]
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[[Category: Bailey, S.]]
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[[Category: Bailey S]]
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[[Category: Hunter, W N.]]
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[[Category: Hunter WN]]
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[[Category: Oxidoreductase]]
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Current revision

SUBSTRATE INTERACTIONS BETWEEN TRYPANOTHIONE REDUCTASE AND N1-GLUTATHIONYLSPERMIDINE DISULPHIDE AT 0.28-NM RESOLUTION

PDB ID 1typ

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