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4gdx
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate complex== | |
| - | + | <StructureSection load='4gdx' size='340' side='right'caption='[[4gdx]], [[Resolution|resolution]] 1.67Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4gdx]] 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=4GDX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GDX FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.67Å</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=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=4gdx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gdx OCA], [https://pdbe.org/4gdx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gdx RCSB], [https://www.ebi.ac.uk/pdbsum/4gdx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gdx ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/GGT1_HUMAN GGT1_HUMAN] Gamma-glutamyl transpeptidase deficiency. The disease is caused by mutations affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/GGT1_HUMAN GGT1_HUMAN] Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Isoform 3 seems to be inactive.<ref>PMID:7689219</ref> <ref>PMID:20622017</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Cahill K]] | ||
| + | [[Category: Chen Y]] | ||
| + | [[Category: Hanigan MH]] | ||
| + | [[Category: Heroux A]] | ||
| + | [[Category: Mooers BHM]] | ||
| + | [[Category: West MB]] | ||
| + | [[Category: Wickham S]] | ||
Current revision
Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate complex
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Categories: Homo sapiens | Large Structures | Cahill K | Chen Y | Hanigan MH | Heroux A | Mooers BHM | West MB | Wickham S
