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1o20

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Current revision (06:39, 25 January 2023) (edit) (undo)
 
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<StructureSection load='1o20' size='340' side='right'caption='[[1o20]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1o20' size='340' side='right'caption='[[1o20]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<table><tr><td colspan='2'>[[1o20]] 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=1O20 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O20 FirstGlance]. <br>
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</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>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1o20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o20 OCA], [https://pdbe.org/1o20 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o20 RCSB], [https://www.ebi.ac.uk/pdbsum/1o20 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o20 ProSAT], [https://www.topsan.org/Proteins/JCSG/1o20 TOPSAN]</span></td></tr>
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<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>
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<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>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PROA_THEMA 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).
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[https://www.uniprot.org/uniprot/PROA_THEMA 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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 43589]]
 
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[[Category: Glutamate-5-semialdehyde dehydrogenase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Structural genomic]]
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[[Category: Thermotoga maritima]]
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[[Category: Gamma-glutamyl phosphate reductase]]
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[[Category: Jcsg]]
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[[Category: Oxidoreductase]]
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[[Category: PSI, Protein structure initiative]]
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[[Category: Tm0293]]
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Current revision

Crystal structure of Gamma-glutamyl phosphate reductase (TM0293) from Thermotoga maritima at 2.00 A resolution

PDB ID 1o20

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