This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4mjb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (16:38, 20 September 2023) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Synechocystis sp. PCC 6803 glutaredoxin A-A79S==
==Synechocystis sp. PCC 6803 glutaredoxin A-A79S==
-
<StructureSection load='4mjb' size='340' side='right' caption='[[4mjb]], [[Resolution|resolution]] 2.11&Aring;' scene=''>
+
<StructureSection load='4mjb' size='340' side='right'caption='[[4mjb]], [[Resolution|resolution]] 2.11&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4mjb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Syny3 Syny3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MJB OCA]. <br>
+
<table><tr><td colspan='2'>[[4mjb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803_substr._Kazusa Synechocystis sp. PCC 6803 substr. Kazusa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MJB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MJB FirstGlance]. <br>
-
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.111&#8491;</td></tr>
-
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qmx|3qmx]], [[4mja|4mja]], [[4mjc|4mjc]], [[4mje|4mje]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ssr2061 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1111708 SYNY3])</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=4mjb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mjb OCA], [https://pdbe.org/4mjb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mjb RCSB], [https://www.ebi.ac.uk/pdbsum/4mjb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mjb ProSAT]</span></td></tr>
-
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
+
</table>
-
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mjb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mjb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mjb RCSB], [http://www.ebi.ac.uk/pdbsum/4mjb PDBsum]</span></td></tr>
+
== Function ==
-
<table>
+
[https://www.uniprot.org/uniprot/GLRX2_SYNY3 GLRX2_SYNY3] Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins (By similarity).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 15: Line 16:
Utility of Synechocystis sp. PCC 6803 glutaredoxin A as a platform to study high-resolution mutagenesis of proteins.,Knaff DB, Sutton RB Front Plant Sci. 2013 Nov 15;4:461. doi: 10.3389/fpls.2013.00461. eCollection, 2013. PMID:24298277<ref>PMID:24298277</ref>
Utility of Synechocystis sp. PCC 6803 glutaredoxin A as a platform to study high-resolution mutagenesis of proteins.,Knaff DB, Sutton RB Front Plant Sci. 2013 Nov 15;4:461. doi: 10.3389/fpls.2013.00461. eCollection, 2013. PMID:24298277<ref>PMID:24298277</ref>
-
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
 +
<div class="pdbe-citations 4mjb" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Syny3]]
+
[[Category: Large Structures]]
-
[[Category: Knaff, D B.]]
+
[[Category: Synechocystis sp. PCC 6803 substr. Kazusa]]
-
[[Category: Sutton, R B.]]
+
[[Category: Knaff DB]]
-
[[Category: Electron transport]]
+
[[Category: Sutton RB]]
-
[[Category: Oxidation/reduction]]
+
-
[[Category: Thioredoxin fold]]
+

Current revision

Synechocystis sp. PCC 6803 glutaredoxin A-A79S

PDB ID 4mjb

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools