1feb: Difference between revisions

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<StructureSection load='1feb' size='340' side='right'caption='[[1feb]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1feb' size='340' side='right'caption='[[1feb]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1feb]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FEB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FEB FirstGlance]. <br>
<table><tr><td colspan='2'>[[1feb]] 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=1FEB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FEB FirstGlance]. <br>
</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>
</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&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fea|1fea]], [[1fec|1fec]]</div></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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Trypanothione-disulfide_reductase Trypanothione-disulfide reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.12 1.8.1.12] </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=1feb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1feb OCA], [https://pdbe.org/1feb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1feb RCSB], [https://www.ebi.ac.uk/pdbsum/1feb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1feb 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=1feb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1feb OCA], [https://pdbe.org/1feb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1feb RCSB], [https://www.ebi.ac.uk/pdbsum/1feb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1feb ProSAT]</span></td></tr>
</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.  
[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]]
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   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fe/1feb_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fe/1feb_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Crithidia fasciculata]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Trypanothione-disulfide reductase]]
[[Category: Karplus P]]
[[Category: Karplus, P]]
[[Category: Strickland C]]
[[Category: Strickland, C]]
[[Category: Fad]]
[[Category: Flavoprotein]]
[[Category: Nadp]]
[[Category: Oxidoreductase]]
[[Category: Redox-active center]]

Latest revision as of 09:37, 30 October 2024

UNLIGANDED CRITHIDIA FASCICULATA TRYPANOTHIONE REDUCTASE AT 2.0 ANGSTROM RESOLUTIONUNLIGANDED CRITHIDIA FASCICULATA TRYPANOTHIONE REDUCTASE AT 2.0 ANGSTROM RESOLUTION

Structural highlights

1feb is a 2 chain structure with sequence from Crithidia fasciculata. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TYTR_CRIFA Trypanothione is the parasite analog of glutathione; this enzyme is the equivalent of glutathione reductase.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1feb, resolution 2.00Å

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