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{{STRUCTURE_4jyw|  PDB=4jyw  |  SCENE=  }}
===X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with CTT1057===


==Function==
==X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with CTT1057==
[[http://www.uniprot.org/uniprot/FOLH1_HUMAN FOLH1_HUMAN]] Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides. In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. Isoform PSM-4 and isoform PSM-5 would appear to be physiologically irrelevant. Involved in prostate tumor progression.  Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC.  
<StructureSection load='4jyw' size='340' side='right'caption='[[4jyw]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4jyw]] is a 1 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=4JYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JYW 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]] 1.73&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=T57:N-{6-[(4-FLUOROBENZOYL)AMINO]HEXANOYL}-L-GAMMA-GLUTAMYL-5-{[(S)-{[(1S)-1,3-DICARBOXYPROPYL]AMINO}(HYDROXY)PHOSPHORYL]OXY}-L-NORVALINE'>T57</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4jyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jyw OCA], [https://pdbe.org/4jyw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jyw RCSB], [https://www.ebi.ac.uk/pdbsum/4jyw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jyw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FOLH1_HUMAN FOLH1_HUMAN] Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides. In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. Isoform PSM-4 and isoform PSM-5 would appear to be physiologically irrelevant. Involved in prostate tumor progression.  Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC.


==About this Structure==
==See Also==
[[4jyw]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JYW OCA].
*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
[[Category: Glutamate carboxypeptidase II]]
__TOC__
[[Category: Barinka, C.]]
</StructureSection>
[[Category: Hydrolase]]
[[Category: Homo sapiens]]
[[Category: Metallopeptidase]]
[[Category: Large Structures]]
[[Category: Barinka C]]
Retrieved from "https://proteopedia.org/4jyw"