4oc3: Difference between revisions

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==X-ray structure of of human glutamate carboxypeptidase II (GCPII) in a complex with CFIBzL, a urea-based inhibitor N~2~-{[(1S)-1-carboxy-2-(furan-2-yl)ethyl]carbamoyl}-N~6~-(4-iodobenzoyl)-L-lysine==
==X-ray structure of of human glutamate carboxypeptidase II (GCPII) in a complex with CFIBzL, a urea-based inhibitor N~2~-{[(1S)-1-carboxy-2-(furan-2-yl)ethyl]carbamoyl}-N~6~-(4-iodobenzoyl)-L-lysine==
<StructureSection load='4oc3' size='340' side='right' caption='[[4oc3]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
<StructureSection load='4oc3' size='340' side='right'caption='[[4oc3]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4oc3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OC3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OC3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4oc3]] 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=4OC3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OC3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2QP:N~2~-{[(1S)-1-CARBOXY-2-(FURAN-2-YL)ETHYL]CARBAMOYL}-N~6~-(4-IODOBENZOYL)-L-LYSINE'>2QP</scene>, <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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.79&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4oc0|4oc0]], [[4oc1|4oc1]], [[4oc2|4oc2]], [[4oc4|4oc4]], [[4oc5|4oc5]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2QP:N~2~-{[(1S)-1-CARBOXY-2-(FURAN-2-YL)ETHYL]CARBAMOYL}-N~6~-(4-IODOBENZOYL)-L-LYSINE'>2QP</scene>, <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=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_carboxypeptidase_II Glutamate carboxypeptidase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.21 3.4.17.21] </span></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=4oc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oc3 OCA], [https://pdbe.org/4oc3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oc3 RCSB], [https://www.ebi.ac.uk/pdbsum/4oc3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oc3 ProSAT]</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=4oc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oc3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oc3 RCSB], [http://www.ebi.ac.uk/pdbsum/4oc3 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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.  
[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.
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4oc3" style="background-color:#fffaf0;"></div>
==See Also==
*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Glutamate carboxypeptidase II]]
[[Category: Homo sapiens]]
[[Category: Barinka, C]]
[[Category: Large Structures]]
[[Category: Byun, Y]]
[[Category: Barinka C]]
[[Category: Cerny, J]]
[[Category: Byun Y]]
[[Category: Lubkowski, J]]
[[Category: Cerny J]]
[[Category: Pavlicek, J]]
[[Category: Lubkowski J]]
[[Category: Pomper, M]]
[[Category: Pavlicek J]]
[[Category: Ptacek, J]]
[[Category: Pomper M]]
[[Category: Skultetyova, L]]
[[Category: Ptacek J]]
[[Category: Hydrolase]]
[[Category: Skultetyova L]]
[[Category: Hydrolase-hydrolase inhibitor complex]]
[[Category: Metallopeptidase]]

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