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3axb
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3axb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AXB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AXB FirstGlance]. <br> | <table><tr><td colspan='2'>[[3axb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AXB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AXB FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <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=3axb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3axb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3axb RCSB], [http://www.ebi.ac.uk/pdbsum/3axb 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=3axb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3axb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3axb RCSB], [http://www.ebi.ac.uk/pdbsum/3axb PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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Crystal Structure of Novel Dye-linked L-Proline Dehydrogenase from Hyperthermophilic Archaeon Aeropyrum pernix.,Sakuraba H, Satomura T, Kawakami R, Kim K, Hara Y, Yoneda K, Ohshima T J Biol Chem. 2012 Jun 8;287(24):20070-80. Epub 2012 Apr 16. PMID:22511758<ref>PMID:22511758</ref> | Crystal Structure of Novel Dye-linked L-Proline Dehydrogenase from Hyperthermophilic Archaeon Aeropyrum pernix.,Sakuraba H, Satomura T, Kawakami R, Kim K, Hara Y, Yoneda K, Ohshima T J Biol Chem. 2012 Jun 8;287(24):20070-80. Epub 2012 Apr 16. PMID:22511758<ref>PMID:22511758</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Aeropyrum pernix]] | [[Category: Aeropyrum pernix]] | ||
| - | [[Category: Hara, Y | + | [[Category: Hara, Y]] |
| - | [[Category: Ohshima, T | + | [[Category: Ohshima, T]] |
| - | [[Category: Sakuraba, H | + | [[Category: Sakuraba, H]] |
| - | [[Category: Satomura, T | + | [[Category: Satomura, T]] |
| - | [[Category: Yoneda, K | + | [[Category: Yoneda, K]] |
[[Category: Dinucleotide-binding fold]] | [[Category: Dinucleotide-binding fold]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
Revision as of 22:49, 3 January 2015
Structure of a dye-linked L-proline dehydrogenase from the aerobic hyperthermophilic archaeon, Aeropyrum pernix
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