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4bqm

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==Crystal structure of human liver-type glutaminase, catalytic domain==
==Crystal structure of human liver-type glutaminase, catalytic domain==
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<StructureSection load='4bqm' size='340' side='right' caption='[[4bqm]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
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<StructureSection load='4bqm' size='340' side='right'caption='[[4bqm]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4bqm]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BQM FirstGlance]. <br>
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<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>
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</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>
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</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>
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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/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>
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<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>
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<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://www.rcsb.org/pdb/explore.do?structureId=4bqm RCSB], [http://www.ebi.ac.uk/pdbsum/4bqm PDBsum]</span></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=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 ==
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[[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>
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[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==
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*[[Glutaminase|Glutaminase]]
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*[[Glutaminase 3D structures|Glutaminase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Glutaminase]]
 
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Ambrosio, A L.B]]
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[[Category: Large Structures]]
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[[Category: Arrowsmith, C H]]
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[[Category: Ambrosio ALB]]
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[[Category: Bountra, C]]
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[[Category: Arrowsmith CH]]
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[[Category: Burgess-Brown, N]]
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[[Category: Bountra C]]
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[[Category: Coutandin, D]]
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[[Category: Burgess-Brown N]]
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[[Category: Delft, F von]]
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[[Category: Coutandin D]]
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[[Category: Dias, S M.G]]
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[[Category: Dias SMG]]
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[[Category: Edwards, A]]
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[[Category: Edwards A]]
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[[Category: Ferreira, I M]]
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[[Category: Ferreira IM]]
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[[Category: Froese, S]]
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[[Category: Froese S]]
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[[Category: Krojer, T]]
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[[Category: Krojer T]]
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[[Category: Strain-Damerell, C]]
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[[Category: Strain-Damerell C]]
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[[Category: Vollmar, M]]
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[[Category: Vollmar M]]
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[[Category: Williams, E]]
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[[Category: Williams E]]
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[[Category: Yue, W W]]
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[[Category: Yue WW]]
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[[Category: Hydrolase]]
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[[Category: Von Delft F]]

Current revision

Crystal structure of human liver-type glutaminase, catalytic domain

PDB ID 4bqm

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