This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1hfu
From Proteopedia
(Difference between revisions)
| (14 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:1hfu.gif|left|200px]]<br /><applet load="1hfu" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1hfu, resolution 1.68Å" /> | ||
| - | '''TYPE-2 CU-DEPLETED LACCASE FROM COPRINUS CINEREUS AT 1.68 A RESOLUTION'''<br /> | ||
| - | == | + | ==TYPE-2 CU-DEPLETED LACCASE FROM COPRINUS CINEREUS at 1.68 A resolution== |
| + | <StructureSection load='1hfu' size='340' side='right'caption='[[1hfu]], [[Resolution|resolution]] 1.68Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1hfu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Coprinopsis_cinerea Coprinopsis cinerea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HFU 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]] 1.68Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900111:2alpha-alpha-mannobiose'>PRD_900111</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=1hfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hfu OCA], [https://pdbe.org/1hfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hfu RCSB], [https://www.ebi.ac.uk/pdbsum/1hfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hfu ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q9Y780_COPCI Q9Y780_COPCI] | ||
| + | == 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/hf/1hfu_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=1hfu ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Laccases (E.C. 1.10.3.2; benzenediol oxygen oxidoreductases) couple the four-electron reduction of dioxygen to water to four one-electron oxidations of a reducing substrate. The three-dimensional structure of the 'blue' multi-copper oxidase laccase from the fungus Coprinus cinereus at 1.68 A reveals the structural basis for isoforms of the type 2 Cu-depleted species. | Laccases (E.C. 1.10.3.2; benzenediol oxygen oxidoreductases) couple the four-electron reduction of dioxygen to water to four one-electron oxidations of a reducing substrate. The three-dimensional structure of the 'blue' multi-copper oxidase laccase from the fungus Coprinus cinereus at 1.68 A reveals the structural basis for isoforms of the type 2 Cu-depleted species. | ||
| - | + | Structure of the laccase from Coprinus cinereus at 1.68 A resolution: evidence for different 'type 2 Cu-depleted' isoforms.,Ducros V, Brzozowski AM, Wilson KS, Ostergaard P, Schneider P, Svendson A, Davies GJ Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):333-6. PMID:11173497<ref>PMID:11173497</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1hfu" style="background-color:#fffaf0;"></div> | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ==See Also== | |
| + | *[[Laccase 3D structures|Laccase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Coprinopsis cinerea]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Brzozowski AM]] | ||
| + | [[Category: Ducros V]] | ||
Current revision
TYPE-2 CU-DEPLETED LACCASE FROM COPRINUS CINEREUS at 1.68 A resolution
| |||||||||||
