2xej
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2xej]] 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=2XEJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XEJ FirstGlance]. <br> | <table><tr><td colspan='2'>[[2xej]] 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=2XEJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XEJ FirstGlance]. <br> | ||
| - | </td></tr><tr><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=OKD:N-({(1S)-1-CARBOXY-5-[4-(2,5,8,11,14-PENTAOXAPENTADEC-1-YL)-1H-1,2,3-TRIAZOL-1-YL]PENTYL}CARBAMOYL)-L-GLUTAMIC+ACID'>OKD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>< | + | </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=OKD:N-({(1S)-1-CARBOXY-5-[4-(2,5,8,11,14-PENTAOXAPENTADEC-1-YL)-1H-1,2,3-TRIAZOL-1-YL]PENTYL}CARBAMOYL)-L-GLUTAMIC+ACID'>OKD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2c6g|2c6g]], [[2c6p|2c6p]], [[2c6c|2c6c]], [[1z8l|1z8l]], [[2jbj|2jbj]], [[2jbk|2jbk]], [[2cij|2cij]], [[2xef|2xef]], [[2xeg|2xeg]], [[2xei|2xei]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2c6g|2c6g]], [[2c6p|2c6p]], [[2c6c|2c6c]], [[1z8l|1z8l]], [[2jbj|2jbj]], [[2jbk|2jbk]], [[2cij|2cij]], [[2xef|2xef]], [[2xeg|2xeg]], [[2xei|2xei]]</td></tr> |
| - | <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> | + | <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> |
| - | <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=2xej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xej OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xej RCSB], [http://www.ebi.ac.uk/pdbsum/2xej PDBsum]</span></td></tr> | + | <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=2xej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xej OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xej RCSB], [http://www.ebi.ac.uk/pdbsum/2xej PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[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]] | ||
| - | [[Category: Barinka, C | + | [[Category: Barinka, C]] |
| - | [[Category: Cocleaza, A | + | [[Category: Cocleaza, A]] |
| - | [[Category: Jorgensen, W L | + | [[Category: Jorgensen, W L]] |
| - | [[Category: Lubkowski, J | + | [[Category: Lubkowski, J]] |
| - | [[Category: Michel, J | + | [[Category: Michel, J]] |
| - | [[Category: Murelli, R | + | [[Category: Murelli, R]] |
| - | [[Category: Spiegel, D A | + | [[Category: Spiegel, D A]] |
| - | [[Category: Zhang, A X | + | [[Category: Zhang, A X]] |
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Metallopeptidase]] | [[Category: Metallopeptidase]] | ||
Revision as of 08:10, 25 December 2014
HUMAN GLUTAMATE CARBOXYPEPTIDASE II IN COMPLEX WITH ARM-M4, UREA-BASED INHIBITOR
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