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==Crystal structure of C-terminal redox domain of APR1 from Arabidopsis thaliana==
==Crystal structure of C-terminal redox domain of APR1 from Arabidopsis thaliana==
<StructureSection load='5yry' size='340' side='right' caption='[[5yry]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='5yry' size='340' side='right'caption='[[5yry]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5yry]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YRY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YRY FirstGlance]. <br>
<table><tr><td colspan='2'>[[5yry]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YRY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YRY FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylyl-sulfate_reductase_(glutathione) Adenylyl-sulfate reductase (glutathione)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.4.9 1.8.4.9] </span></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]] 2.698&#8491;</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=5yry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yry OCA], [http://pdbe.org/5yry PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yry RCSB], [http://www.ebi.ac.uk/pdbsum/5yry PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yry 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=5yry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yry OCA], [https://pdbe.org/5yry PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yry RCSB], [https://www.ebi.ac.uk/pdbsum/5yry PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yry ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/APR1_ARATH APR1_ARATH]] Reduces sulfate for Cys biosynthesis. Substrate preference is adenosine-5'-phosphosulfate (APS) >> 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Uses glutathione or DTT as source of protons.  
[https://www.uniprot.org/uniprot/APR1_ARATH APR1_ARATH] Reduces sulfate for Cys biosynthesis. Substrate preference is adenosine-5'-phosphosulfate (APS) >> 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Uses glutathione or DTT as source of protons.
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Hsu, C H]]
[[Category: Arabidopsis thaliana]]
[[Category: Aps reductase]]
[[Category: Large Structures]]
[[Category: Oxidoreductase]]
[[Category: Hsu CH]]
[[Category: Redox domain]]
[[Category: Sulfer assimilatory]]

Latest revision as of 10:24, 27 March 2024

Crystal structure of C-terminal redox domain of APR1 from Arabidopsis thaliana

5yry, resolution 2.70Å

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