1o20: Difference between revisions
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==Crystal structure of Gamma-glutamyl phosphate reductase (TM0293) from Thermotoga maritima at 2.00 A resolution== | ==Crystal structure of Gamma-glutamyl phosphate reductase (TM0293) from Thermotoga maritima at 2.00 A resolution== | ||
<StructureSection load='1o20' size='340' side='right' caption='[[1o20]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1o20' size='340' side='right'caption='[[1o20]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1o20]] 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=1O20 OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[1o20]] 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=1O20 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1O20 FirstGlance]. <br> | ||
</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> | </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 id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM0293 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM0293 ([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/Glutamate-5-semialdehyde_dehydrogenase Glutamate-5-semialdehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.41 1.2.1.41] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate-5-semialdehyde_dehydrogenase Glutamate-5-semialdehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.41 1.2.1.41] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1o20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o20 OCA], [http://pdbe.org/1o20 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o20 RCSB], [http://www.ebi.ac.uk/pdbsum/1o20 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o20 ProSAT], [http://www.topsan.org/Proteins/JCSG/1o20 TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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[[Category: Atcc 43589]] | [[Category: Atcc 43589]] | ||
[[Category: Glutamate-5-semialdehyde dehydrogenase]] | [[Category: Glutamate-5-semialdehyde dehydrogenase]] | ||
[[Category: Large Structures]] | |||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
[[Category: Gamma-glutamyl phosphate reductase]] | [[Category: Gamma-glutamyl phosphate reductase]] | ||
Revision as of 12:01, 2 December 2020
Crystal structure of Gamma-glutamyl phosphate reductase (TM0293) from Thermotoga maritima at 2.00 A resolutionCrystal structure of Gamma-glutamyl phosphate reductase (TM0293) from Thermotoga maritima at 2.00 A resolution
Structural highlights
Function[PROA_THEMA] Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. |
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