This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2xej
From Proteopedia
(Difference between revisions)
| (2 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
==Human glutamate carboxypeptidase II in complex with ARM-M4, urea- based inhibitor== | ==Human glutamate carboxypeptidase II in complex with ARM-M4, urea- based inhibitor== | ||
| - | <StructureSection load='2xej' size='340' side='right' caption='[[2xej]], [[Resolution|resolution]] 1.78Å' scene=''> | + | <StructureSection load='2xej' size='340' side='right'caption='[[2xej]], [[Resolution|resolution]] 1.78Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2xej]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2xej]] 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=2XEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XEJ 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=MAN:ALPHA-D-MANNOSE'>MAN</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 | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.78Å</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=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></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=2xej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xej OCA], [https://pdbe.org/2xej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xej RCSB], [https://www.ebi.ac.uk/pdbsum/2xej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xej ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == 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. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 32: | Line 31: | ||
==See Also== | ==See Also== | ||
| - | *[[Carboxypeptidase|Carboxypeptidase]] | + | *[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Barinka | + | [[Category: Barinka C]] |
| - | [[Category: Cocleaza | + | [[Category: Cocleaza A]] |
| - | [[Category: Jorgensen | + | [[Category: Jorgensen WL]] |
| - | [[Category: Lubkowski | + | [[Category: Lubkowski J]] |
| - | [[Category: Michel | + | [[Category: Michel J]] |
| - | [[Category: Murelli | + | [[Category: Murelli R]] |
| - | [[Category: Spiegel | + | [[Category: Spiegel DA]] |
| - | [[Category: Zhang | + | [[Category: Zhang AX]] |
| - | + | ||
| - | + | ||
Current revision
Human glutamate carboxypeptidase II in complex with ARM-M4, urea- based inhibitor
| |||||||||||
Categories: Homo sapiens | Large Structures | Barinka C | Cocleaza A | Jorgensen WL | Lubkowski J | Michel J | Murelli R | Spiegel DA | Zhang AX
