1j5p: 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 [http://en.wikipedia.org/wiki/ | <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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J5P FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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"><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 | <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='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='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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j5p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1j5p RCSB], [http://www.ebi.ac.uk/pdbsum/1j5p PDBsum], [http://www.topsan.org/Proteins/JCSG/1j5p TOPSAN]</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=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://www.topsan.org/Proteins/JCSG/1j5p TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== 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> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Atcc 43589]] | |||
[[Category: L-aspartate oxidase]] | [[Category: L-aspartate oxidase]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
[[Category: Aspartate dehydrogenase]] | [[Category: Aspartate dehydrogenase]] | ||
Revision as of 01:19, 12 September 2015
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
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
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