4mcp

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==A high resolution structure of human glutamate carboxypeptidase II (GCPII) in complex with folyl-gamma-L-glutamic acid (pteroyldi-gamma-L-glutamic acid)==
==A high resolution structure of human glutamate carboxypeptidase II (GCPII) in complex with folyl-gamma-L-glutamic acid (pteroyldi-gamma-L-glutamic acid)==
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<StructureSection load='4mcp' size='340' side='right' caption='[[4mcp]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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<StructureSection load='4mcp' size='340' side='right'caption='[[4mcp]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4mcp]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MCP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MCP FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4mcp]] 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=4MCP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MCP FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=28Z:N-(4-{[(2-AMINO-4-OXO-3,4-DIHYDROPTERIDIN-6-YL)METHYL]AMINO}BENZOYL)-L-GAMMA-GLUTAMYL-L-GLUTAMIC+ACID'>28Z</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=MAN:ALPHA-D-MANNOSE'>MAN</scene><br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mcq|4mcq]], [[4mcr|4mcr]], [[4mcs|4mcs]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=28Z:N-(4-{[(2-AMINO-4-OXO-3,4-DIHYDROPTERIDIN-6-YL)METHYL]AMINO}BENZOYL)-L-GAMMA-GLUTAMYL-L-GLUTAMIC+ACID'>28Z</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><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'>[https://proteopedia.org/fgij/fg.htm?mol=4mcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mcp OCA], [https://pdbe.org/4mcp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mcp RCSB], [https://www.ebi.ac.uk/pdbsum/4mcp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mcp ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mcp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mcp RCSB], [http://www.ebi.ac.uk/pdbsum/4mcp PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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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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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>
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<div class="pdbe-citations 4mcp" 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: Lubkowski, J.]]
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[[Category: Barinka C]]
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[[Category: Navratil, M.]]
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[[Category: Lubkowski J]]
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[[Category: Hydrolase]]
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[[Category: Navratil M]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]
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[[Category: Metallopeptidase]]
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Current revision

A high resolution structure of human glutamate carboxypeptidase II (GCPII) in complex with folyl-gamma-L-glutamic acid (pteroyldi-gamma-L-glutamic acid)

PDB ID 4mcp

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OCA

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