1dz0
From Proteopedia
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| - | [[Image:1dz0.gif|left|200px]]<br /><applet load="1dz0" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1dz0, resolution 1.75Å" /> | ||
| - | '''REDUCED AZURIN II FROM ALCALIGENES XYLOSOXIDANS'''<br /> | ||
| - | == | + | ==REDUCED AZURIN II FROM ALCALIGENES XYLOSOXIDANS== |
| + | <StructureSection load='1dz0' size='340' side='right'caption='[[1dz0]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1dz0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Achromobacter_xylosoxidans Achromobacter xylosoxidans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DZ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DZ0 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]] 1.75Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</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=1dz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dz0 OCA], [https://pdbe.org/1dz0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dz0 RCSB], [https://www.ebi.ac.uk/pdbsum/1dz0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dz0 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/AZUR2_ALCXX AZUR2_ALCXX] Transfers electrons from cytochrome c551 to cytochrome oxidase. | ||
| + | == 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/dz/1dz0_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=1dz0 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Crystallographic structures of oxidized and reduced forms of azurin II are reported at 1.75 A resolution. Data were collected using one crystal in each case and by translating the crystal after each oscillation range to minimize photoreduction. Very small differences are observed at the Cu site upon reduction and these cannot be determined with confidence at current resolution. A comparison with the three-dimensional EXAFS reveals a good correspondence for all the ligand distances except for Cu-His46, where a larger deviation of approximately 0.12-0.18 A is observed, indicating that this ligand is more tightly restrained in the crystallographic refinement at the current resolution. | Crystallographic structures of oxidized and reduced forms of azurin II are reported at 1.75 A resolution. Data were collected using one crystal in each case and by translating the crystal after each oscillation range to minimize photoreduction. Very small differences are observed at the Cu site upon reduction and these cannot be determined with confidence at current resolution. A comparison with the three-dimensional EXAFS reveals a good correspondence for all the ligand distances except for Cu-His46, where a larger deviation of approximately 0.12-0.18 A is observed, indicating that this ligand is more tightly restrained in the crystallographic refinement at the current resolution. | ||
| - | + | Structures of oxidized and reduced azurin II from Alcaligenes xylosoxidans at 1.75 A resolution.,Dodd FE, Abraham ZH, Eady RR, Hasnain SS Acta Crystallogr D Biol Crystallogr. 2000 Jun;56(Pt 6):690-6. PMID:10818345<ref>PMID:10818345</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1dz0" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Azurin 3D structures|Azurin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Achromobacter xylosoxidans]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Abraham ZHL]] | ||
| + | [[Category: Dodd FE]] | ||
| + | [[Category: Eady RR]] | ||
| + | [[Category: Hasnain SS]] | ||
Current revision
REDUCED AZURIN II FROM ALCALIGENES XYLOSOXIDANS
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