6i35

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Current revision (11:45, 24 January 2024) (edit) (undo)
 
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<StructureSection load='6i35' size='340' side='right'caption='[[6i35]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='6i35' size='340' side='right'caption='[[6i35]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6i35]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I35 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6I35 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6i35]] is a 4 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=6I35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6I35 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=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PLG:N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE]'>PLG</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&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6i33|6i33]]</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=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PLG:N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE]'>PLG</scene></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/Glycine_dehydrogenase_(decarboxylating) Glycine dehydrogenase (decarboxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.4.2 1.4.4.2] </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=6i35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i35 OCA], [https://pdbe.org/6i35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6i35 RCSB], [https://www.ebi.ac.uk/pdbsum/6i35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6i35 ProSAT]</span></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=6i35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i35 OCA], [http://pdbe.org/6i35 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6i35 RCSB], [http://www.ebi.ac.uk/pdbsum/6i35 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6i35 ProSAT]</span></td></tr>
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</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/GCSP_HUMAN GCSP_HUMAN]] Atypical glycine encephalopathy;Infantile glycine encephalopathy;Neonatal glycine encephalopathy. The disease is caused by mutations affecting the gene represented in this entry.
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[https://www.uniprot.org/uniprot/GCSP_HUMAN GCSP_HUMAN] Atypical glycine encephalopathy;Infantile glycine encephalopathy;Neonatal glycine encephalopathy. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/GCSP_HUMAN GCSP_HUMAN]] The glycine cleavage system catalyzes the degradation of glycine. The P protein (GLDC) binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (GCSH).<ref>PMID:1993704</ref> <ref>PMID:1996985</ref> <ref>PMID:28244183</ref>
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[https://www.uniprot.org/uniprot/GCSP_HUMAN GCSP_HUMAN] The glycine cleavage system catalyzes the degradation of glycine. The P protein (GLDC) binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (GCSH).<ref>PMID:1993704</ref> <ref>PMID:1996985</ref> <ref>PMID:28244183</ref>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Kapp, U]]
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[[Category: Kapp U]]
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[[Category: Laer, B Van]]
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[[Category: Leonard G]]
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[[Category: Leonard, G]]
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[[Category: Mueller-Dieckmann C]]
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[[Category: Mueller-Dieckmann, C]]
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[[Category: Van Laer B]]
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[[Category: Glycine cleavage system p-protein]]
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[[Category: Glycine decarboxylase]]
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[[Category: Mitochondrial]]
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[[Category: Oxidoreductase]]
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Current revision

Crystal structure of human glycine decarboxylase (P-protein) bound with pyridoxyl-glycine-5'-monophosphate

PDB ID 6i35

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OCA

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