1j5p: Difference between revisions

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<StructureSection load='1j5p' size='340' side='right'caption='[[1j5p]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1j5p' size='340' side='right'caption='[[1j5p]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1j5p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1J5P FirstGlance]. <br>
<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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM1643 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</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>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-aspartate_oxidase L-aspartate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.16 1.4.3.16] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1j5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j5p OCA], [http://pdbe.org/1j5p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1j5p RCSB], [http://www.ebi.ac.uk/pdbsum/1j5p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1j5p ProSAT], [http://www.topsan.org/Proteins/JCSG/1j5p TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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>
[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: Structural genomic]]
[[Category: Thermotoga maritima]]
[[Category: Aspartate dehydrogenase]]
[[Category: Jcsg]]
[[Category: Oxidoreductase]]
[[Category: PSI, Protein structure initiative]]
[[Category: Tm1643]]

Revision as of 09:39, 25 January 2023

Crystal structure of aspartate dehydrogenase (TM1643) from Thermotoga maritima at 1.9 A resolutionCrystal structure of aspartate dehydrogenase (TM1643) from Thermotoga maritima at 1.9 A resolution

Structural highlights

1j5p is a 1 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

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.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Yang Z, Savchenko A, Yakunin A, Zhang R, Edwards A, Arrowsmith C, Tong L. Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643. J Biol Chem. 2003 Mar 7;278(10):8804-8. Epub 2002 Dec 21. PMID:12496312 doi:10.1074/jbc.M211892200

1j5p, resolution 1.90Å

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