4oc3
From Proteopedia
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<StructureSection load='4oc3' size='340' side='right'caption='[[4oc3]], [[Resolution|resolution]] 1.79Å' scene=''> | <StructureSection load='4oc3' size='340' side='right'caption='[[4oc3]], [[Resolution|resolution]] 1.79Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[4oc3]] is a 1 chain structure with sequence from [ | + | <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=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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.79Å</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='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'>[ | + | |
</table> | </table> | ||
== Function == | == 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. |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
- | *[[Carboxypeptidase|Carboxypeptidase]] | + | *[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Homo sapiens]] |
- | + | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Barinka | + | [[Category: Barinka C]] |
- | [[Category: Byun | + | [[Category: Byun Y]] |
- | [[Category: Cerny | + | [[Category: Cerny J]] |
- | [[Category: Lubkowski | + | [[Category: Lubkowski J]] |
- | [[Category: Pavlicek | + | [[Category: Pavlicek J]] |
- | [[Category: Pomper | + | [[Category: Pomper M]] |
- | [[Category: Ptacek | + | [[Category: Ptacek J]] |
- | [[Category: Skultetyova | + | [[Category: Skultetyova L]] |
- | + | ||
- | + | ||
- | + |
Current revision
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
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Categories: Homo sapiens | Large Structures | Barinka C | Byun Y | Cerny J | Lubkowski J | Pavlicek J | Pomper M | Ptacek J | Skultetyova L