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| | <StructureSection load='3fcx' size='340' side='right'caption='[[3fcx]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='3fcx' size='340' side='right'caption='[[3fcx]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3fcx]] is a 2 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=3FCX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FCX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3fcx]] is a 2 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=3FCX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FCX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.5Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ESD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/S-formylglutathione_hydrolase S-formylglutathione hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.12 3.1.2.12] </span></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=3fcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fcx OCA], [https://pdbe.org/3fcx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fcx RCSB], [https://www.ebi.ac.uk/pdbsum/3fcx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fcx ProSAT]</span></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=3fcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fcx OCA], [https://pdbe.org/3fcx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fcx RCSB], [https://www.ebi.ac.uk/pdbsum/3fcx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fcx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/ESTD_HUMAN ESTD_HUMAN]] Serine hydrolase involved in the detoxification of formaldehyde.<ref>PMID:4768551</ref> <ref>PMID:3770744</ref>
| + | [https://www.uniprot.org/uniprot/ESTD_HUMAN ESTD_HUMAN] Serine hydrolase involved in the detoxification of formaldehyde.<ref>PMID:4768551</ref> <ref>PMID:3770744</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: S-formylglutathione hydrolase]]
| + | [[Category: Li Y]] |
| - | [[Category: Li, Y]] | + | [[Category: Liu ZJ]] |
| - | [[Category: Liu, Z J]] | + | [[Category: Shaw N]] |
| - | [[Category: Shaw, N]] | + | [[Category: Song G]] |
| - | [[Category: Song, G]] | + | [[Category: Wu D]] |
| - | [[Category: Wu, D]] | + | [[Category: Zhang D]] |
| - | [[Category: Zhang, D]] | + | |
| - | [[Category: Cytoplasm]]
| + | |
| - | [[Category: Cytoplasmic vesicle]]
| + | |
| - | [[Category: Esterase]]
| + | |
| - | [[Category: Genetic marker]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Polymorphism]]
| + | |
| - | [[Category: Retinoblastoma]]
| + | |
| - | [[Category: Serine esterase]]
| + | |
| Structural highlights
Function
ESTD_HUMAN Serine hydrolase involved in the detoxification of formaldehyde.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Retinoblastoma (RB), a carcinoma of the retina, is caused by mutations in the long arm of chromosome 13, band 13q14. The esterase D (ESD) gene maps at a similar location as the RB gene locus and therefore serves as a potential marker for the prognosis of retinoblastoma. Because very little is known about the structure and function of ESD, we determined the 3-dimensional structure of the enzyme at 1.5 A resolution using X-ray crystallography. ESD shows a single domain with an alpha/beta-hydrolase fold. A number of insertions are observed in the canonical alpha/beta-hydrolase fold. The active site is located in a positively charged, shallow cleft on the surface lined by a number of aromatic residues. Superimposition studies helped identify the typical catalytic triad residues--Ser-153, His264, and Asp230--involved in catalysis. Mutagenesis of any of the catalytic triad residues to alanine abolished the enzyme activity. Backbone amides of Leu54 and Met150 are involved in the formation of the oxyanion hole. Interestingly, a M150A mutation increased the enzyme activity by 62%. The structure of human ESD determined in this study will aid the elucidation of the physiological role of the enzyme in the human body and will assist in the early diagnosis of retinoblastoma.
Crystal structure of human esterase D: a potential genetic marker of retinoblastoma.,Wu D, Li Y, Song G, Zhang D, Shaw N, Liu ZJ FASEB J. 2009 May;23(5):1441-6. Epub 2009 Jan 6. PMID:19126594[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hopkinson DA, Mestriner MA, Cortner J, Harris H. Esterase D: a new human polymorphism. Ann Hum Genet. 1973 Oct;37(2):119-37. PMID:4768551
- ↑ Eiberg H, Mohr J. Identity of the polymorphisms for esterase D and S-formylglutathione hydrolase in red blood cells. Hum Genet. 1986 Oct;74(2):174-5. PMID:3770744
- ↑ Wu D, Li Y, Song G, Zhang D, Shaw N, Liu ZJ. Crystal structure of human esterase D: a potential genetic marker of retinoblastoma. FASEB J. 2009 May;23(5):1441-6. Epub 2009 Jan 6. PMID:19126594 doi:10.1096/fj.08-125286
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