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1q7l
From Proteopedia
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| - | [[Image:1q7l.gif|left|200px]] | ||
| - | + | ==Zn-binding domain of the T347G mutant of human aminoacylase-I== | |
| - | + | <StructureSection load='1q7l' size='340' side='right'caption='[[1q7l]], [[Resolution|resolution]] 1.40Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1q7l]] is a 4 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=1Q7L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q7L 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]] 1.4Å</td></tr> | |
| - | --> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</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=1q7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q7l OCA], [https://pdbe.org/1q7l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q7l RCSB], [https://www.ebi.ac.uk/pdbsum/1q7l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q7l ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/ACY1_HUMAN ACY1_HUMAN] Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D) [MIM:[https://omim.org/entry/609924 609924]. ACY1D results in a metabolic disorder manifesting with encephalopathy, unspecific psychomotor delay, psychomotor delay with atrophy of the vermis and syringomyelia, marked muscular hypotonia or normal clinical features. Epileptic seizures are a frequent feature. All affected individuals exhibit markedly increased urinary excretion of several N-acetylated amino acids.<ref>PMID:16465618</ref> <ref>PMID:16274666</ref> <ref>PMID:17562838</ref> <ref>PMID:21414403</ref> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ACY1_HUMAN ACY1_HUMAN] Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate).<ref>PMID:12933810</ref> | ||
| + | == 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/q7/1q7l_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/main_output.php?pdb_ID=1q7l ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | + | ==See Also== | |
| - | + | *[[Aminoacylase 3D structures|Aminoacylase 3D structures]] | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Alary | + | [[Category: Alary A]] |
| - | [[Category: Cygler | + | [[Category: Cygler M]] |
| - | [[Category: Hecker | + | [[Category: Hecker R]] |
| - | [[Category: Lindner | + | [[Category: Lindner HA]] |
| - | [[Category: Lunin | + | [[Category: Lunin VV]] |
| - | [[Category: Menard | + | [[Category: Menard R]] |
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Current revision
Zn-binding domain of the T347G mutant of human aminoacylase-I
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Categories: Homo sapiens | Large Structures | Alary A | Cygler M | Hecker R | Lindner HA | Lunin VV | Menard R

