1aps

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{{Seed}}
 
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[[Image:1aps.png|left|200px]]
 
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==THREE-DIMENSIONAL STRUCTURE OF ACYLPHOSPHATASE. REFINEMENT AND STRUCTURE ANALYSIS==
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The line below this paragraph, containing "STRUCTURE_1aps", creates the "Structure Box" on the page.
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<StructureSection load='1aps' size='340' side='right'caption='[[1aps]]' 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'>[[1aps]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1APS 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">Solution NMR</td></tr>
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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=1aps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aps OCA], [https://pdbe.org/1aps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aps RCSB], [https://www.ebi.ac.uk/pdbsum/1aps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aps ProSAT]</span></td></tr>
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{{STRUCTURE_1aps| PDB=1aps | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ACYP2_HORSE ACYP2_HORSE] Its physiological role is not yet clear.
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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/ap/1aps_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=1aps ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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We report here the complete determination of the solution structure of acylphosphatase, a small enzyme that catalyses the hydrolysis of organic acylphosphates, as determined by distance geometry methods based on nuclear magnetic resonance information. A non-standard strategy for the distance geometry calculations was used and is described here some detail. The five best structures were then refined by restrained energy minimization and molecular dynamics in order to explore the conformational space consistent with the experimental data. We address the question of whether the solution structure of acylphosphatase follows the general principles of protein structure, i.e. those learned from analysing crystal structures. Static and dynamic features are discussed in detail. An uncommon beta-alpha-beta motif, so far found only in procarboxypeptidase B and in an RNA-binding protein, is present in acylphosphatase.
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===THREE-DIMENSIONAL STRUCTURE OF ACYLPHOSPHATASE. REFINEMENT AND STRUCTURE ANALYSIS===
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Three-dimensional structure of acylphosphatase. Refinement and structure analysis.,Pastore A, Saudek V, Ramponi G, Williams RJ J Mol Biol. 1992 Mar 20;224(2):427-40. PMID:1313885<ref>PMID:1313885</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_1313885}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1aps" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 1313885 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_1313885}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1APS is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APS OCA].
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==Reference==
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<ref group="xtra">PMID:1313885</ref><references group="xtra"/>
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[[Category: Acylphosphatase]]
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[[Category: Equus caballus]]
[[Category: Equus caballus]]
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[[Category: Pastore, A.]]
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[[Category: Large Structures]]
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[[Category: Ramponi, G.]]
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[[Category: Pastore A]]
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[[Category: Saudek, V.]]
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[[Category: Ramponi G]]
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[[Category: Williams, R J.P.]]
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[[Category: Saudek V]]
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[[Category: Williams RJP]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 21:11:19 2009''
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Current revision

THREE-DIMENSIONAL STRUCTURE OF ACYLPHOSPHATASE. REFINEMENT AND STRUCTURE ANALYSIS

PDB ID 1aps

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