1o20

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1o20" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o20, resolution 2.00&Aring;" /> '''Crystal structure of...)
Current revision (06:39, 25 January 2023) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1o20.gif|left|200px]]<br /><applet load="1o20" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1o20, resolution 2.00&Aring;" />
 
-
'''Crystal structure of Gamma-glutamyl phosphate reductase (TM0293) from Thermotoga maritima at 2.00 A resolution'''<br />
 
-
==About this Structure==
+
==Crystal structure of Gamma-glutamyl phosphate reductase (TM0293) from Thermotoga maritima at 2.00 A resolution==
-
1O20 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O20 OCA].
+
<StructureSection load='1o20' size='340' side='right'caption='[[1o20]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-
 
+
== Structural highlights ==
-
==Reference==
+
<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>
-
Crystal structure of gamma-glutamyl phosphate reductase (TM0293) from Thermotoga maritima at 2.0 A resolution., Page R, Nelson MS, von Delft F, Elsliger MA, Canaves JM, Brinen LS, Dai X, Deacon AM, Floyd R, Godzik A, Grittini C, Grzechnik SK, Jaroszewski L, Klock HE, Koesema E, Kovarik JS, Kreusch A, Kuhn P, Lesley SA, McMullan D, McPhillips TM, Miller MD, Morse A, Moy K, Ouyang J, Robb A, Rodrigues K, Schwarzenbacher R, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, Wang X, West B, Wolf G, Hodgson KO, Wooley J, Wilson IA, Proteins. 2004 Jan 1;54(1):157-61. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14705032 14705032]
+
</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>
-
[[Category: Glutamate-5-semialdehyde dehydrogenase]]
+
<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>
-
[[Category: Single protein]]
+
</table>
 +
== Function ==
 +
[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 ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o2/1o20_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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/main_output.php?pdb_ID=1o20 ConSurf].
 +
<div style="clear:both"></div>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
-
[[Category: JCSG, Joint.Center.for.Structural.Genomics.]]
 
-
[[Category: gamma-glutamyl phosphate reductase]]
 
-
[[Category: jcsg]]
 
-
[[Category: joint center for structural genomics]]
 
-
[[Category: protein structure initiative]]
 
-
[[Category: psi]]
 
-
[[Category: structural genomics]]
 
-
[[Category: tm0293]]
 
- 
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:44:30 2007''
 

Current revision

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

PDB ID 1o20

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools