3gro
From Proteopedia
(Difference between revisions)
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- | + | ==Human palmitoyl-protein thioesterase 1== | |
- | + | <StructureSection load='3gro' size='340' side='right' caption='[[3gro]], [[Resolution|resolution]] 2.53Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[3gro]] is a 2 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=3GRO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GRO FirstGlance]. <br> | |
- | + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene><br> | |
- | + | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |
- | + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPT1, PPT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | |
- | == | + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Palmitoyl-protein_hydrolase Palmitoyl-protein hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.22 3.1.2.22] </span></td></tr> |
- | [[3gro]] is a 2 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=3GRO OCA]. | + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3gro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gro OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gro RCSB], [http://www.ebi.ac.uk/pdbsum/3gro PDBsum]</span></td></tr> |
+ | <table> | ||
+ | == Disease == | ||
+ | [[http://www.uniprot.org/uniprot/PPT1_HUMAN PPT1_HUMAN]] CLN1 disease. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:7637805</ref> <ref>PMID:9425237</ref> <ref>PMID:9664077</ref> <ref>PMID:11506414</ref> <ref>PMID:19201763</ref> <ref>PMID:21990111</ref> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/PPT1_HUMAN PPT1_HUMAN]] Removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. Prefers acyl chain lengths of 14 to 18 carbons. | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gr/3gro_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
+ | *[[Palmitoyl protein thioesterase|Palmitoyl protein thioesterase]] | ||
*[[Thioesterase|Thioesterase]] | *[[Thioesterase|Thioesterase]] | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Palmitoyl-protein hydrolase]] | [[Category: Palmitoyl-protein hydrolase]] |
Revision as of 13:22, 29 September 2014
Human palmitoyl-protein thioesterase 1
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Categories: Homo sapiens | Palmitoyl-protein hydrolase | Arrowsmith, C H. | Bochkarev, A. | Bountra, C. | Cossar, D. | Dobrovetsky, E. | Dong, A. | Edwards, A M. | Park, H. | SGC, Structural Genomics Consortium. | Seitova, A. | Tempel, W. | Tong, Y. | Weigelt, J. | Disease mutation | Disulfide bond | Glycoprotein | Hydrolase | Lysosome | Neurodegeneration | Neuronal ceroid lipofuscinosis | Sensory transduction | Sgc | Structural genomics consortium | Vision