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==Crystal structure of human liver-type glutaminase, catalytic domain==
==Crystal structure of human liver-type glutaminase, catalytic domain==
<StructureSection load='4bqm' size='340' side='right' caption='[[4bqm]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
<StructureSection load='4bqm' size='340' side='right'caption='[[4bqm]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4bqm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BQM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BQM FirstGlance]. <br>
<table><tr><td colspan='2'>[[4bqm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BQM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BQM 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>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.18&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutaminase Glutaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.2 3.5.1.2] </span></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=EDO:1,2-ETHANEDIOL'>EDO</scene></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=4bqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bqm OCA], [http://pdbe.org/4bqm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bqm RCSB], [http://www.ebi.ac.uk/pdbsum/4bqm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bqm ProSAT]</span></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=4bqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bqm OCA], [https://pdbe.org/4bqm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bqm RCSB], [https://www.ebi.ac.uk/pdbsum/4bqm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bqm ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/GLSL_HUMAN GLSL_HUMAN]] Plays an important role in the regulation of glutamine catabolism. Promotes mitochondrial respiration and increases ATP generation in cells by catalyzing the synthesis of glutamate and alpha-ketoglutarate. Increases cellular anti-oxidant function via NADH and glutathione production. May play a role in preventing tumor proliferation.<ref>PMID:20378837</ref>
[https://www.uniprot.org/uniprot/GLSL_HUMAN GLSL_HUMAN] Plays an important role in the regulation of glutamine catabolism. Promotes mitochondrial respiration and increases ATP generation in cells by catalyzing the synthesis of glutamate and alpha-ketoglutarate. Increases cellular anti-oxidant function via NADH and glutathione production. May play a role in preventing tumor proliferation.<ref>PMID:20378837</ref>  


==See Also==
==See Also==
*[[Glutaminase|Glutaminase]]
*[[Glutaminase 3D structures|Glutaminase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Glutaminase]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Ambrosio, A L.B]]
[[Category: Ambrosio ALB]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith CH]]
[[Category: Bountra, C]]
[[Category: Bountra C]]
[[Category: Burgess-Brown, N]]
[[Category: Burgess-Brown N]]
[[Category: Coutandin, D]]
[[Category: Coutandin D]]
[[Category: Delft, F von]]
[[Category: Dias SMG]]
[[Category: Dias, S M.G]]
[[Category: Edwards A]]
[[Category: Edwards, A]]
[[Category: Ferreira IM]]
[[Category: Ferreira, I M]]
[[Category: Froese S]]
[[Category: Froese, S]]
[[Category: Krojer T]]
[[Category: Krojer, T]]
[[Category: Strain-Damerell C]]
[[Category: Strain-Damerell, C]]
[[Category: Vollmar M]]
[[Category: Vollmar, M]]
[[Category: Williams E]]
[[Category: Williams, E]]
[[Category: Yue WW]]
[[Category: Yue, W W]]
[[Category: Von Delft F]]
[[Category: Hydrolase]]

Latest revision as of 11:56, 20 December 2023

Crystal structure of human liver-type glutaminase, catalytic domain

4bqm, resolution 2.18Å

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