2c6p

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==Membrane-bound glutamate carboxypeptidase II (GCPII) in complex with phosphate anion==
==Membrane-bound glutamate carboxypeptidase II (GCPII) in complex with phosphate anion==
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<StructureSection load='2c6p' size='340' side='right' caption='[[2c6p]], [[Resolution|resolution]] 2.39&Aring;' scene=''>
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<StructureSection load='2c6p' size='340' side='right'caption='[[2c6p]], [[Resolution|resolution]] 2.39&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2c6p]] 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=2C6P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C6P FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2c6p]] 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=2C6P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C6P 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=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=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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]] 2.39&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1z8l|1z8l]], [[2c6c|2c6c]], [[2c6g|2c6g]]</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=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=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=2c6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c6p OCA], [https://pdbe.org/2c6p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c6p RCSB], [https://www.ebi.ac.uk/pdbsum/2c6p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c6p ProSAT]</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=2c6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c6p OCA], [http://pdbe.org/2c6p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c6p RCSB], [http://www.ebi.ac.uk/pdbsum/2c6p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2c6p 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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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<jmolCheckbox>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c6/2c6p_consurf.spt"</scriptWhenChecked>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c6/2c6p_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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==See Also==
==See Also==
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*[[Carboxypeptidase|Carboxypeptidase]]
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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: Human]]
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[[Category: Large Structures]]
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[[Category: Barinka, C]]
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[[Category: Barinka C]]
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[[Category: Hilgenfeld, R]]
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[[Category: Hilgenfeld R]]
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[[Category: Konvalinka, J]]
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[[Category: Konvalinka J]]
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[[Category: Li, W]]
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[[Category: Li W]]
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[[Category: Majer, P]]
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[[Category: Majer P]]
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[[Category: Mesters, J R]]
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[[Category: Mesters JR]]
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[[Category: Slusher, B S]]
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[[Category: Slusher BS]]
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[[Category: Tsukamoto, T]]
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[[Category: Tsukamoto T]]
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[[Category: Alternative splicing]]
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[[Category: Antigen]]
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[[Category: Carboxypeptidase]]
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[[Category: Dipeptidase]]
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[[Category: Glycoprotein]]
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[[Category: Hydrolase]]
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[[Category: Metal-binding]]
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[[Category: Metalloprotease]]
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[[Category: Multifunctional enzyme]]
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[[Category: Naaladase]]
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[[Category: Neurodegenerative disease]]
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[[Category: Peptidase]]
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[[Category: Polymorphism]]
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[[Category: Prostate cancer]]
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[[Category: Psma]]
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[[Category: Signal-anchor]]
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[[Category: Transmembrane]]
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[[Category: Zinc]]
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Current revision

Membrane-bound glutamate carboxypeptidase II (GCPII) in complex with phosphate anion

PDB ID 2c6p

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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