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1j5p
From Proteopedia
(Difference between revisions)
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<StructureSection load='1j5p' size='340' side='right'caption='[[1j5p]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1j5p' size='340' side='right'caption='[[1j5p]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1j5p]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1j5p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J5P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J5P FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></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=1j5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j5p OCA], [https://pdbe.org/1j5p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j5p RCSB], [https://www.ebi.ac.uk/pdbsum/1j5p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j5p ProSAT], [https://www.topsan.org/Proteins/JCSG/1j5p TOPSAN]</span></td></tr> | |
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/ASPD_THEMA ASPD_THEMA] Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate. Does not show aspartate oxidase activity. Is also able to catalyze the reverse reaction, i.e. the reductive amination of oxaloacetate.<ref>PMID:12496312</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Atcc 43589]] | ||
| - | [[Category: L-aspartate oxidase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Thermotoga maritima]] |
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Revision as of 06:39, 25 January 2023
Crystal structure of aspartate dehydrogenase (TM1643) from Thermotoga maritima at 1.9 A resolution
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