4jz0: Difference between revisions

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~~'''Unreleased structure'''~~

~~The entry~~ 4jz0 is ~~ON HOLD~~

==X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with CTT1055==

== Structural highlights ==

<table><tr><td colspan='2'>[[4jz0]] 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=4JZ0 OCA]. For a guided tour on the structure components use [https://proteopedia.org/fgij/fg.htm?mol=4JZ0 FirstGlance].

</td></tr><tr id='method'><td class="sblockLbl">[[Empirical_models|Method:]]</td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.83Å</td></tr>

<tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</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=T01:N-(4-FLUOROBENZOYL)-L-GAMMA-GLUTAMYL-O-[(S)-{[(1S)-1,3-DICARBOXYPROPYL]AMINO}(HYDROXY)PHOSPHORYL]-L-SERINE'>T01</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[https://proteopedia.org/fgij/fg.htm?mol=4jz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jz0 OCA], [https://pdbe.org/4jz0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jz0 RCSB], [https://www.ebi.ac.uk/pdbsum/4jz0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jz0 ProSAT]</td></tr>

</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.

~~Authors~~: ~~Barinka, C.~~

==See Also==

*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]

~~Description~~: ~~X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with CTT1055~~

__TOC__

</StructureSection>

[[Category: Homo sapiens]]

[[Category: Large Structures]]

[[Category: Barinka C]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4jz0 is ON HOLD
+==X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with CTT1055==
+<StructureSection load='4jz0' size='340' side='right'caption='[[4jz0]], [[Resolution|resolution]] 1.83&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4jz0]] 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=4JZ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JZ0 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.83&#8491;</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=T01:N-(4-FLUOROBENZOYL)-L-GAMMA-GLUTAMYL-O-[(S)-{[(1S)-1,3-DICARBOXYPROPYL]AMINO}(HYDROXY)PHOSPHORYL]-L-SERINE'>T01</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4jz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jz0 OCA], [https://pdbe.org/4jz0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jz0 RCSB], [https://www.ebi.ac.uk/pdbsum/4jz0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jz0 ProSAT]</span></td></tr>
+</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.
-Authors: Barinka, C.
+==See Also==
+*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
-Description: X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with CTT1055
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Barinka C]]