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2act
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:2act.png|left|200px]] | ||
| - | + | ==CRYSTALLOGRAPHIC REFINEMENT OF THE STRUCTURE OF ACTINIDIN AT 1.7 ANGSTROMS RESOLUTION BY FAST FOURIER LEAST-SQUARES METHODS== | |
| - | + | <StructureSection load='2act' size='340' side='right'caption='[[2act]], [[Resolution|resolution]] 1.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2act]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinidia_chinensis Actinidia chinensis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1act 1act]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ACT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ACT 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]] 1.7Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</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=2act FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2act OCA], [https://pdbe.org/2act PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2act RCSB], [https://www.ebi.ac.uk/pdbsum/2act PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2act ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/ACTN_ACTCC ACTN_ACTCC] Cysteine protease responsible for the cleavage of kiwellin into kissper and KiTH.<ref>PMID:18442249</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/ac/2act_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=2act ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Actinidia chinensis]] | [[Category: Actinidia chinensis]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | + | [[Category: Baker EN]] | |
| - | + | ||
Current revision
CRYSTALLOGRAPHIC REFINEMENT OF THE STRUCTURE OF ACTINIDIN AT 1.7 ANGSTROMS RESOLUTION BY FAST FOURIER LEAST-SQUARES METHODS
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