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2xei

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2xei]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XEI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XEI FirstGlance]. <br>
<table><tr><td colspan='2'>[[2xei]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XEI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XEI FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ARK:N-({(1S)-5-[4-({2-[2-({2,4-BIS[HYDROXY(OXO)AMMONIO]PHENYL}AMINO)ETHOXY]ETHOXY}METHYL)-1H-1,2,3-TRIAZOL-1-YL]-1-CARBOXYPENTYL}CARBAMOYL)-L-GLUTAMIC+ACID'>ARK</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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene><br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ARK:N-({(1S)-5-[4-({2-[2-({2,4-BIS[HYDROXY(OXO)AMMONIO]PHENYL}AMINO)ETHOXY]ETHOXY}METHYL)-1H-1,2,3-TRIAZOL-1-YL]-1-CARBOXYPENTYL}CARBAMOYL)-L-GLUTAMIC+ACID'>ARK</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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2c6g|2c6g]], [[2c6c|2c6c]], [[2c6p|2c6p]], [[1z8l|1z8l]], [[2jbj|2jbj]], [[2jbk|2jbk]], [[2cij|2cij]], [[2xej|2xej]], [[2xef|2xef]], [[2xeg|2xeg]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2c6g|2c6g]], [[2c6c|2c6c]], [[2c6p|2c6p]], [[1z8l|1z8l]], [[2jbj|2jbj]], [[2jbk|2jbk]], [[2cij|2cij]], [[2xej|2xej]], [[2xef|2xef]], [[2xeg|2xeg]]</td></tr>
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<tr><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='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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xei OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xei RCSB], [http://www.ebi.ac.uk/pdbsum/2xei PDBsum]</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=2xei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xei OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xei RCSB], [http://www.ebi.ac.uk/pdbsum/2xei PDBsum]</span></td></tr>
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<table>
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</table>
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== 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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Glutamate carboxypeptidase II]]
[[Category: Glutamate carboxypeptidase II]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Barinka, C.]]
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[[Category: Barinka, C]]
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[[Category: Cocleaza, A.]]
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[[Category: Cocleaza, A]]
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[[Category: Jorgensen, W L.]]
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[[Category: Jorgensen, W L]]
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[[Category: Lubkowski, J.]]
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[[Category: Lubkowski, J]]
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[[Category: Michel, J.]]
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[[Category: Michel, J]]
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[[Category: Murelli, R P.]]
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[[Category: Murelli, R P]]
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[[Category: Spiegel, D A.]]
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[[Category: Spiegel, D A]]
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[[Category: Zhang, A X.]]
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[[Category: Zhang, A X]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Metallopeptidase]]
[[Category: Metallopeptidase]]

Revision as of 13:55, 25 December 2014

HUMAN GLUTAMATE CARBOXYPEPTIDASE II IN COMPLEX WITH ANTIBODY-RECRUITING MOLECULE ARM-P2

2xei, resolution 1.69Å

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