1feb: Difference between revisions

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==UNLIGANDED CRITHIDIA FASCICULATA TRYPANOTHIONE REDUCTASE AT 2.0 ANGSTROM RESOLUTION==
==UNLIGANDED CRITHIDIA FASCICULATA TRYPANOTHIONE REDUCTASE AT 2.0 ANGSTROM RESOLUTION==
<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 with sequence from [http://en.wikipedia.org/wiki/Crifa Crifa]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FEB FirstGlance]. <br>
<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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FEB FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fea|1fea]], [[1fec|1fec]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fea|1fea]], [[1fec|1fec]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TR1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5656 CRIFA])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypanothione-disulfide_reductase Trypanothione-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.12 1.8.1.12] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypanothione-disulfide_reductase Trypanothione-disulfide reductase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1feb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1feb OCA], [http://pdbe.org/1feb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1feb RCSB], [http://www.ebi.ac.uk/pdbsum/1feb PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1feb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1feb OCA], [http://pdbe.org/1feb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1feb RCSB], [http://www.ebi.ac.uk/pdbsum/1feb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1feb ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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     <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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=1feb ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>


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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Crifa]]
[[Category: Trypanothione-disulfide reductase]]
[[Category: Trypanothione-disulfide reductase]]
[[Category: Karplus, P]]
[[Category: Karplus, P]]

Revision as of 13:34, 13 September 2017

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. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:Trypanothione-disulfide reductase, with EC number 1.8.1.12
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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