1q7l

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{{Seed}}
 
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[[Image:1q7l.png|left|200px]]
 
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==Zn-binding domain of the T347G mutant of human aminoacylase-I==
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The line below this paragraph, containing "STRUCTURE_1q7l", creates the "Structure Box" on the page.
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<StructureSection load='1q7l' size='340' side='right'caption='[[1q7l]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
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<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>
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{{STRUCTURE_1q7l| PDB=1q7l | SCENE= }}
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<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>
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</table>
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== Disease ==
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[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>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q7/1q7l_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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===Zn-binding domain of the T347G mutant of human aminoacylase-I===
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==See Also==
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*[[Aminoacylase 3D structures|Aminoacylase 3D structures]]
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== References ==
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_12933810}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 12933810 is the PubMed ID number.
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</StructureSection>
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{{ABSTRACT_PUBMED_12933810}}
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==Disease==
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Known disease associated with this structure: Aminoacylase 1 deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=104620 104620]]
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==About this Structure==
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1Q7L is a [[Protein complex]] structure of sequences 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=1Q7L OCA].
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==Reference==
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Essential roles of zinc ligation and enzyme dimerization for catalysis in the aminoacylase-1/M20 family., Lindner HA, Lunin VV, Alary A, Hecker R, Cygler M, Menard R, J Biol Chem. 2003 Nov 7;278(45):44496-504. Epub 2003 Aug 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12933810 12933810]
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[[Category: Aminoacylase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Alary, A.]]
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[[Category: Alary A]]
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[[Category: Cygler, M.]]
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[[Category: Cygler M]]
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[[Category: Hecker, R.]]
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[[Category: Hecker R]]
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[[Category: Lindner, H A.]]
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[[Category: Lindner HA]]
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[[Category: Lunin, V V.]]
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[[Category: Lunin VV]]
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[[Category: Menard, R.]]
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[[Category: Menard R]]
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[[Category: Aminoacylase-1]]
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[[Category: Catalysis]]
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[[Category: Enzyme dimerization]]
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[[Category: Site-directed mutagenesis]]
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[[Category: Structure comparison]]
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[[Category: Zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:34:29 2008''
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Current revision

Zn-binding domain of the T347G mutant of human aminoacylase-I

PDB ID 1q7l

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