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4p4f

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==X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with a phosphoramidate inhibitor NC-2-40==
==X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with a phosphoramidate inhibitor NC-2-40==
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<StructureSection load='4p4f' size='340' side='right' caption='[[4p4f]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
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<StructureSection load='4p4f' size='340' side='right'caption='[[4p4f]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4p4f]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P4F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P4F FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4p4f]] 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=4P4F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P4F FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2GB:N-[(S)-(BIPHENYL-4-YLMETHOXY)(HYDROXY)PHOSPHORYL]-L-GLUTAMIC+ACID'>2GB</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=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>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2GB:N-[(S)-(BIPHENYL-4-YLMETHOXY)(HYDROXY)PHOSPHORYL]-L-GLUTAMIC+ACID'>2GB</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=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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4p4b|4p4b]], [[4p4d|4p4d]], [[4p4e|4p4e]], [[4p4i|4p4i]], [[4p4j|4p4j]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4p4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p4f OCA], [https://pdbe.org/4p4f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p4f RCSB], [https://www.ebi.ac.uk/pdbsum/4p4f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p4f ProSAT]</span></td></tr>
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<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>
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<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=4p4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p4f OCA], [http://pdbe.org/4p4f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p4f RCSB], [http://www.ebi.ac.uk/pdbsum/4p4f PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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.
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[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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 4p4f" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4p4f" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Glutamate carboxypeptidase II]]
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[[Category: Homo sapiens]]
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[[Category: Barinka, C]]
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[[Category: Large Structures]]
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[[Category: Hydrolase]]
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[[Category: Barinka C]]
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[[Category: Naaladase]]
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[[Category: Phosphoramidate]]
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[[Category: Prostate-specific membrane antigen]]
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Current revision

X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with a phosphoramidate inhibitor NC-2-40

PDB ID 4p4f

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