4zbk: Difference between revisions
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==Crystal Structure of human GGT1 in complex with GGsTop inhibitor== | ==Crystal Structure of human GGT1 in complex with GGsTop inhibitor== | ||
<StructureSection load='4zbk' size='340' side='right' caption='[[4zbk]], [[Resolution|resolution]] 2.18Å' scene=''> | <StructureSection load='4zbk' size='340' side='right'caption='[[4zbk]], [[Resolution|resolution]] 2.18Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4zbk]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4zbk]] 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=4ZBK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZBK FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4M8:(2S)-2-AMINO-4-[(S)-HYDROXY(METHOXY)PHOSPHORYL]BUTANOIC+ACID'>4M8</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.18Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4M8:(2S)-2-AMINO-4-[(S)-HYDROXY(METHOXY)PHOSPHORYL]BUTANOIC+ACID'>4M8</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4zbk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zbk OCA], [https://pdbe.org/4zbk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zbk RCSB], [https://www.ebi.ac.uk/pdbsum/4zbk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zbk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == 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 == | == 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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Hanigan M]] | ||
[[Category: | [[Category: Terzyan S]] | ||