4x3r

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<StructureSection load='4x3r' size='340' side='right'caption='[[4x3r]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
<StructureSection load='4x3r' size='340' side='right'caption='[[4x3r]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4x3r]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X3R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X3R FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4x3r]] 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=4X3R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X3R 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=686:N-({(1S)-5-[(4-BROMOBENZYL)({6-[4-(4-{4-[4-CARBOXY-3-(6-HYDROXY-3-OXO-3H-XANTHEN-9-YL)BENZOYL]PIPERAZIN-1-YL}PHENYL)PIPERAZIN-1-YL]PYRIDIN-3-YL}CARBONYL)AMINO]-1-CARBOXYPENTYL}CARBAMOYL)-L-GLUTAMIC+ACID'>686</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=686:N-({(1S)-5-[(4-BROMOBENZYL)({6-[4-(4-{4-[4-CARBOXY-3-(6-HYDROXY-3-OXO-3H-XANTHEN-9-YL)BENZOYL]PIPERAZIN-1-YL}PHENYL)PIPERAZIN-1-YL]PYRIDIN-3-YL}CARBONYL)AMINO]-1-CARBOXYPENTYL}CARBAMOYL)-L-GLUTAMIC+ACID'>686</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FOLH1, FOLH, NAALAD1, PSM, PSMA, GIG27 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4x3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x3r OCA], [https://pdbe.org/4x3r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x3r RCSB], [https://www.ebi.ac.uk/pdbsum/4x3r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x3r 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=4x3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x3r OCA], [http://pdbe.org/4x3r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x3r RCSB], [http://www.ebi.ac.uk/pdbsum/4x3r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x3r ProSAT]</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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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Glutamate carboxypeptidase II]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Konvalinka, J]]
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[[Category: Konvalinka J]]
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[[Category: Tykvart, J]]
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[[Category: Tykvart J]]
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[[Category: Glycoprotein]]
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[[Category: Hydrolase]]
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[[Category: Inhibitor]]
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[[Category: Metallopeptidase]]
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Revision as of 21:10, 12 April 2023

Avi-GCPII structure in complex with FITC-conjugated GCPII-specific inhibitor

PDB ID 4x3r

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