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3bhx
From Proteopedia
(Difference between revisions)
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==X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with a transition state analog of Asp-Glu== | ==X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with a transition state analog of Asp-Glu== | ||
| - | <StructureSection load='3bhx' size='340' side='right' caption='[[3bhx]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='3bhx' size='340' side='right'caption='[[3bhx]], [[Resolution|resolution]] 1.60Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3bhx]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3bhx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BHX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BHX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BHX:(2S)-2-{[(S)-(2-CARBOXYETHYL)(HYDROXY)PHOSPHORYL]METHYL}PENTANEDIOIC+ACID'>BHX</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= | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BHX:(2S)-2-{[(S)-(2-CARBOXYETHYL)(HYDROXY)PHOSPHORYL]METHYL}PENTANEDIOIC+ACID'>BHX</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> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bi0|3bi0]], [[3bi1|3bi1]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3bi0|3bi0]], [[3bi1|3bi1]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FOLH1, FOLH, NAALAD1, PSM, PSMA ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FOLH1, FOLH, NAALAD1, PSM, PSMA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutamate_carboxypeptidase_II Glutamate carboxypeptidase II], with EC number [https://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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bhx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bhx OCA], [https://pdbe.org/3bhx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bhx RCSB], [https://www.ebi.ac.uk/pdbsum/3bhx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bhx ProSAT]</span></td></tr> |
</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]] | ||
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==See Also== | ==See Also== | ||
| - | *[[Carboxypeptidase|Carboxypeptidase]] | + | *[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Glutamate carboxypeptidase II]] | [[Category: Glutamate carboxypeptidase II]] | ||
[[Category: Human]] | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Barinka, C]] | [[Category: Barinka, C]] | ||
[[Category: Lubkowski, J]] | [[Category: Lubkowski, J]] | ||
Revision as of 10:42, 12 January 2022
X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with a transition state analog of Asp-Glu
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Categories: Glutamate carboxypeptidase II | Human | Large Structures | Barinka, C | Lubkowski, J | Dipeptidase | Folate hydrolase | Glutamate carboxypeptidase ii | Glycoprotein | Hydrolase | Metal-binding | Metallopeptidase | Metalloprotease | Multifunctional enzyme | Naaladase | Prostate specific membrane antigen | Protease | Signal-anchor | Transmembrane
