6i33: Difference between revisions
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The entry | ==Crystal structure of human glycine decarboxylase (P-protein)== | ||
<StructureSection load='6i33' size='340' side='right'caption='[[6i33]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6i33]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I33 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6I33 FirstGlance]. <br> | |||
</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=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | |||
[[Category: | <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> | ||
<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=6i33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i33 OCA], [http://pdbe.org/6i33 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6i33 RCSB], [http://www.ebi.ac.uk/pdbsum/6i33 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6i33 ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[[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. | |||
== Function == | |||
[[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> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Kapp, U]] | |||
[[Category: Laer, B Van]] | |||
[[Category: Leonard, G]] | |||
[[Category: Mueller-Dieckmann, C]] | |||
[[Category: Glycine cleavage system p-protein]] | |||
[[Category: Glycine decarboxylase]] | |||
[[Category: Mitochondrial]] | |||
[[Category: Oxidoreductase]] | |||
Revision as of 15:18, 20 November 2019
Crystal structure of human glycine decarboxylase (P-protein)
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