1qj4

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[[Image:1qj4.png|left|200px]]
 
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==HYDROXYNITRILE-LYASE FROM HEVEA BRASILIENSIS AT ATOMIC RESOLUTION==
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The line below this paragraph, containing "STRUCTURE_1qj4", creates the "Structure Box" on the page.
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<StructureSection load='1qj4' size='340' side='right'caption='[[1qj4]], [[Resolution|resolution]] 1.10&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'>[[1qj4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hevea_brasiliensis Hevea brasiliensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QJ4 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]] 1.1&#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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1qj4| PDB=1qj4 | 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=1qj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qj4 OCA], [https://pdbe.org/1qj4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qj4 RCSB], [https://www.ebi.ac.uk/pdbsum/1qj4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qj4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HNL_HEVBR HNL_HEVBR] Involved in cyanogenesis, the release of HCN from injured tissues. Decomposes a varieties of (R) or (S) cyanohydrins into HCN and the corresponding aldehydes and ketones. The natural substrate of this enzyme is (S)-acetone cyanohydrin.
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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/qj/1qj4_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=1qj4 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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The X-ray crystal structure of native hydroxynitrile lyase from Hevea brasiliensis (Hb-HNL) has been determined at 1.1 A resolution. It refined to a final R of 11.5% for all data and an Rfree of 14.4%. The favorable data-to-parameter ratio at atomic resolution made the refinement of individual anisotropic displacement parameters possible. The data also allowed a clear distinction of the alternate orientations of all histidine and the majority of asparagine and glutamine side chains. A number of hydrogen atoms, including one on the imidazole of the mechanistically important His-235, became visible as peaks in a difference electron density map. The structure revealed a discretely disordered sidechain of Ser-80, which is part of the putative catalytic triad. Analysis of the anisotropy indicated an increased mobility of residues near the entrance to the active site and within the active site.
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===HYDROXYNITRILE-LYASE FROM HEVEA BRASILIENSIS AT ATOMIC RESOLUTION===
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Atomic resolution crystal structure of hydroxynitrile lyase from Hevea brasiliensis.,Gruber K, Gugganig M, Wagner UG, Kratky C Biol Chem. 1999 Jul-Aug;380(7-8):993-1000. PMID:10494852<ref>PMID:10494852</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_10494852}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1qj4" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 10494852 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10494852}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[1qj4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hevea_brasiliensis Hevea brasiliensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJ4 OCA].
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==Reference==
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<ref group="xtra">PMID:10494852</ref><ref group="xtra">PMID:10548044</ref><ref group="xtra">PMID:8805565</ref><ref group="xtra">PMID:15299689</ref><ref group="xtra">PMID:8621461</ref><references group="xtra"/>
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[[Category: Hevea brasiliensis]]
[[Category: Hevea brasiliensis]]
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[[Category: Hydroxynitrilase]]
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[[Category: Large Structures]]
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[[Category: Gruber, K.]]
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[[Category: Gruber K]]
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[[Category: Gugganig, M.]]
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[[Category: Gugganig M]]
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[[Category: Kratky, C.]]
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[[Category: Kratky C]]
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[[Category: Cyanhydrin formation]]
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[[Category: Cyanogenesis]]
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[[Category: Lyase]]
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[[Category: Oxynitrilase]]
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Current revision

HYDROXYNITRILE-LYASE FROM HEVEA BRASILIENSIS AT ATOMIC RESOLUTION

PDB ID 1qj4

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