3sjg: Difference between revisions

No edit summary
No edit summary
 
(3 intermediate revisions by the same user not shown)
Line 1: Line 1:
==Human glutamate carboxypeptidase II (E424A inactive mutant ) in complex with N-acetyl-aspartyl-aminooctanoic acid==
==Human glutamate carboxypeptidase II (E424A inactive mutant ) in complex with N-acetyl-aspartyl-aminooctanoic acid==
<StructureSection load='3sjg' size='340' side='right' caption='[[3sjg]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
<StructureSection load='3sjg' size='340' side='right'caption='[[3sjg]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3sjg]] 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=3SJG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SJG FirstGlance]. <br>
<table><tr><td colspan='2'>[[3sjg]] 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=3SJG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SJG FirstGlance]. <br>
</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=SDR:(2S)-2-[(N-ACETYL-L-ALPHA-ASPARTYL)AMINO]NONANOIC+ACID'>SDR</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sje|3sje]], [[3sjf|3sjf]], [[3sjx|3sjx]]</td></tr>
<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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SDR:(2S)-2-[(N-ACETYL-L-ALPHA-ASPARTYL)AMINO]NONANOIC+ACID'>SDR</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FOLH, FOLH1, GIG27, NAALAD1, PSM, PSMA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3sjg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sjg OCA], [https://pdbe.org/3sjg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sjg RCSB], [https://www.ebi.ac.uk/pdbsum/3sjg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sjg ProSAT]</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 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=3sjg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sjg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sjg RCSB], [http://www.ebi.ac.uk/pdbsum/3sjg PDBsum]</span></td></tr>
</table>
</table>
== 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 ==
Line 17: Line 18:
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 3sjg" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Carboxypeptidase|Carboxypeptidase]]
*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Glutamate carboxypeptidase II]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Alquicer, G]]
[[Category: Large Structures]]
[[Category: Barinka, C]]
[[Category: Alquicer G]]
[[Category: Byun, Y]]
[[Category: Barinka C]]
[[Category: Kim, H]]
[[Category: Byun Y]]
[[Category: Konvalinka, J]]
[[Category: Kim H]]
[[Category: Lubkowski, J]]
[[Category: Konvalinka J]]
[[Category: Mease, R]]
[[Category: Lubkowski J]]
[[Category: Mlcochova, P]]
[[Category: Mease R]]
[[Category: Navratil, M]]
[[Category: Mlcochova P]]
[[Category: Nemcova, A]]
[[Category: Navratil M]]
[[Category: Plechanovova, A]]
[[Category: Nemcova A]]
[[Category: Pomper, M]]
[[Category: Plechanovova A]]
[[Category: Rulisek, L]]
[[Category: Pomper M]]
[[Category: Skultetyova, L]]
[[Category: Rulisek L]]
[[Category: Hydrolase]]
[[Category: Skultetyova L]]
[[Category: Hydrolase-hydrolase inhibitor complex]]
[[Category: Metallopeptidase]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA