This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4gg2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (15:45, 14 March 2024) (edit) (undo)
 
(5 intermediate revisions not shown.)
Line 1: Line 1:
-
{{STRUCTURE_4gg2| PDB=4gg2 | SCENE= }}
 
-
===The crystal structure of glutamate-bound human gamma-glutamyltranspeptidase 1===
 
-
==Disease==
+
==The crystal structure of glutamate-bound human gamma-glutamyltranspeptidase 1==
-
[[http://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.
+
<StructureSection load='4gg2' size='340' side='right'caption='[[4gg2]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
-
 
+
== Structural highlights ==
-
==Function==
+
<table><tr><td colspan='2'>[[4gg2]] 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=4GG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GG2 FirstGlance]. <br>
-
[[http://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>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.21&#8491;</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=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-
==About this Structure==
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4gg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gg2 OCA], [https://pdbe.org/4gg2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gg2 RCSB], [https://www.ebi.ac.uk/pdbsum/4gg2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gg2 ProSAT]</span></td></tr>
-
[[4gg2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Zasmidium_angulare Zasmidium angulare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GG2 OCA].
+
</table>
-
 
+
== Disease ==
-
==Reference==
+
[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.
-
<references group="xtra"/><references/>
+
== 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: Homo sapiens]]
-
[[Category: Zasmidium angulare]]
+
[[Category: Large Structures]]
-
[[Category: Cahill, K.]]
+
[[Category: Cahill K]]
-
[[Category: Chen, Y.]]
+
[[Category: Chen Y]]
-
[[Category: Hanigan, M H.]]
+
[[Category: Hanigan MH]]
-
[[Category: Heroux, A.]]
+
[[Category: Heroux A]]
-
[[Category: Mooers, B H.M.]]
+
[[Category: Mooers BHM]]
-
[[Category: West, M B.]]
+
[[Category: West MB]]
-
[[Category: Wickham, S.]]
+
[[Category: Wickham S]]
-
[[Category: Exterior cell surface]]
+
-
[[Category: Glutathionine metabolism]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: N-glycosylation]]
+
-
[[Category: Ntn-hydrolyase]]
+

Current revision

The crystal structure of glutamate-bound human gamma-glutamyltranspeptidase 1

PDB ID 4gg2

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4gg2"
Personal tools