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.


1jeh

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:15, 25 October 2023) (edit) (undo)
 
(One intermediate revision not shown.)
Line 3: Line 3:
<StructureSection load='1jeh' size='340' side='right'caption='[[1jeh]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='1jeh' size='340' side='right'caption='[[1jeh]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[1jeh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JEH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JEH FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[1jeh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JEH 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyl_dehydrogenase Dihydrolipoyl dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.4 1.8.1.4] </span></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='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=1jeh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jeh OCA], [http://pdbe.org/1jeh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jeh RCSB], [http://www.ebi.ac.uk/pdbsum/1jeh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jeh 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=1jeh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jeh OCA], [https://pdbe.org/1jeh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jeh RCSB], [https://www.ebi.ac.uk/pdbsum/1jeh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jeh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/DLDH_YEAST DLDH_YEAST]] Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes. This includes the pyruvate dehydrogenase complex, which catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). Acts also as component of the glycine cleavage system (glycine decarboxylase complex), which catalyzes the degradation of glycine.
+
[https://www.uniprot.org/uniprot/DLDH_YEAST DLDH_YEAST] Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes. This includes the pyruvate dehydrogenase complex, which catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). Acts also as component of the glycine cleavage system (glycine decarboxylase complex), which catalyzes the degradation of glycine.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 36: Line 36:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Dihydrolipoyl dehydrogenase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
-
[[Category: Reed, J]]
+
[[Category: Reed J]]
-
[[Category: Sekigushi, T]]
+
[[Category: Sekigushi T]]
-
[[Category: Suzuki, K]]
+
[[Category: Suzuki K]]
-
[[Category: Takenaka, A]]
+
[[Category: Takenaka A]]
-
[[Category: Toyoda, T]]
+
[[Category: Toyoda T]]
-
[[Category: 2-oxoglutarate dehydrogenase complex]]
+
-
[[Category: Oxidoreductase]]
+
-
[[Category: Pyruvate dehydrogenase complex]]
+

Current revision

CRYSTAL STRUCTURE OF YEAST E3, LIPOAMIDE DEHYDROGENASE

PDB ID 1jeh

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1jeh"
Personal tools