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3rbu
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==N-terminally AviTEV-tagged Human Glutamate Carboxypeptidase II in complex with 2-PMPA== | |
| + | <StructureSection load='3rbu' size='340' side='right'caption='[[3rbu]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3rbu]] 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=3RBU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RBU 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]] 1.6Å</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=G88:(2S)-2-(PHOSPHONOMETHYL)PENTANEDIOIC+ACID'>G88</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3rbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rbu OCA], [https://pdbe.org/3rbu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rbu RCSB], [https://www.ebi.ac.uk/pdbsum/3rbu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rbu 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. | ||
| - | + | ==See Also== | |
| - | + | *[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]] | |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Barinka C]] | ||
| + | [[Category: Knedlik T]] | ||
| + | [[Category: Konvalinka J]] | ||
| + | [[Category: Lubkowski J]] | ||
| + | [[Category: Sacha P]] | ||
| + | [[Category: Starkova J]] | ||
| + | [[Category: Tykvart J]] | ||
Current revision
N-terminally AviTEV-tagged Human Glutamate Carboxypeptidase II in complex with 2-PMPA
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