1vlu: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(One intermediate revision by the same user not shown)
Line 1: Line 1:


==Crystal structure of Gamma-glutamyl phosphate reductase (yor323c) from Saccharomyces cerevisiae at 2.40 A resolution==
==Crystal structure of Gamma-glutamyl phosphate reductase (yor323c) from Saccharomyces cerevisiae at 2.40 A resolution==
<StructureSection load='1vlu' size='340' side='right' caption='[[1vlu]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
<StructureSection load='1vlu' size='340' side='right'caption='[[1vlu]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1vlu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VLU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VLU FirstGlance]. <br>
<table><tr><td colspan='2'>[[1vlu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VLU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VLU FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vlu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vlu OCA], [https://pdbe.org/1vlu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vlu RCSB], [https://www.ebi.ac.uk/pdbsum/1vlu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vlu ProSAT], [https://www.topsan.org/Proteins/JCSG/1vlu TOPSAN]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PRO2, YOR323C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vlu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vlu OCA], [http://pdbe.org/1vlu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vlu RCSB], [http://www.ebi.ac.uk/pdbsum/1vlu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1vlu ProSAT], [http://www.topsan.org/Proteins/JCSG/1vlu TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PROA_YEAST PROA_YEAST]] Catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.  
[https://www.uniprot.org/uniprot/PROA_YEAST PROA_YEAST] Catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 24: Line 21:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Glutamate-5-semialdehyde dehydrogenase]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Structural genomic]]
[[Category: Gamma-glutamyl phosphate reductase]]
[[Category: Jcsg]]
[[Category: Oxidoreductase]]
[[Category: PSI, Protein structure initiative]]
[[Category: Yor323c]]

Latest revision as of 09:41, 25 January 2023

Crystal structure of Gamma-glutamyl phosphate reductase (yor323c) from Saccharomyces cerevisiae at 2.40 A resolutionCrystal structure of Gamma-glutamyl phosphate reductase (yor323c) from Saccharomyces cerevisiae at 2.40 A resolution

Structural highlights

1vlu is a 2 chain structure with sequence from Saccharomyces cerevisiae. 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

PROA_YEAST Catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.

Evolutionary Conservation

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

1vlu, resolution 2.29Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA