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2cij

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[[Image:2cij.gif|left|200px]]<br />
 
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<applet load="2cij" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2cij, resolution 2.40&Aring;" />
 
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'''MEMBRANE-BOUND GLUTAMATE CARBOXYPEPTIDASE II (GCPII) WITH BOUND METHIONINE'''<br />
 
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==About this Structure==
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==membrane-bound glutamate carboxypeptidase II (GCPII) with bound methionine==
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2CIJ is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with NAG, ZN, CA, CL and MET as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[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]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CIJ OCA]].
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<StructureSection load='2cij' size='340' side='right'caption='[[2cij]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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[[Category: Glutamate carboxypeptidase II]]
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== Structural highlights ==
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[[Category: Homo sapiens]]
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<table><tr><td colspan='2'>[[2cij]] 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=2CIJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CIJ FirstGlance]. <br>
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[[Category: Single protein]]
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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]] 2.4&#8491;</td></tr>
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[[Category: Barinka, C.]]
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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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</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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[[Category: Hilgenfeld, R.]]
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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=2cij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cij OCA], [https://pdbe.org/2cij PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cij RCSB], [https://www.ebi.ac.uk/pdbsum/2cij PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cij ProSAT]</span></td></tr>
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[[Category: Konvalinka, J.]]
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</table>
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[[Category: Majer, P.]]
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== Function ==
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[[Category: Mesters, J.R.]]
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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.
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[[Category: Mlcochova, P.]]
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== Evolutionary Conservation ==
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[[Category: Plechanovova, A.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Rulisek, L.]]
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Check<jmol>
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[[Category: Slusher, B.S.]]
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<jmolCheckbox>
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[[Category: CA]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ci/2cij_consurf.spt"</scriptWhenChecked>
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[[Category: CL]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: MET]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: NAG]]
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</jmolCheckbox>
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[[Category: ZN]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2cij ConSurf].
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[[Category: alternative splicing]]
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<div style="clear:both"></div>
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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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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 17:09:16 2007''
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==See Also==
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*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Barinka C]]
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[[Category: Hilgenfeld R]]
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[[Category: Konvalinka J]]
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[[Category: Majer P]]
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[[Category: Mesters JR]]
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[[Category: Mlcochova P]]
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[[Category: Plechanovova A]]
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[[Category: Rulisek L]]
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[[Category: Slusher BS]]

Current revision

membrane-bound glutamate carboxypeptidase II (GCPII) with bound methionine

PDB ID 2cij

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