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| | <StructureSection load='3kw7' size='340' side='right'caption='[[3kw7]], [[Resolution|resolution]] 3.44Å' scene=''> | | <StructureSection load='3kw7' size='340' side='right'caption='[[3kw7]], [[Resolution|resolution]] 3.44Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3kw7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Trametes Trametes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KW7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3KW7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3kw7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trametes_sp._AH28-2 Trametes sp. AH28-2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KW7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KW7 FirstGlance]. <br> |
| - | </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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.44Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Laccase Laccase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.3.2 1.10.3.2] </span></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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3kw7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kw7 OCA], [http://pdbe.org/3kw7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kw7 RCSB], [http://www.ebi.ac.uk/pdbsum/3kw7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kw7 ProSAT]</span></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=3kw7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kw7 OCA], [https://pdbe.org/3kw7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kw7 RCSB], [https://www.ebi.ac.uk/pdbsum/3kw7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kw7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q5I7J0_9APHY Q5I7J0_9APHY] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Laccase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Trametes]] | + | [[Category: Trametes sp. AH28-2]] |
| - | [[Category: Ge, H H]] | + | [[Category: Ge HH]] |
| - | [[Category: Niu, L W]] | + | [[Category: Niu LW]] |
| - | [[Category: Teng, M K]] | + | [[Category: Teng MK]] |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
Q5I7J0_9APHY
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Fungal laccases are oxidoreductases that belong to the multinuclear copper-containing oxidases. They are able to oxidize a wide range of substrates, preferably phenolic compounds, which makes them suitable for employment in the bioremediation of soil and water as well as in other biotechnological applications. Here, the structural analysis of natural laccase B (LacB) from Trametes sp. AH28-2 is presented. This structure provides the opportunity to study the natural post-translational modifications of the enzyme. The overall fold shows a high homology to those of previously analyzed laccases with known three-dimensional structure. However, LacB contains a new structural element, a protruding loop near the substrate-binding site, compared with the previously reported laccase structures. This unique structural feature may be involved in modulation of the substrate recognition of LacB.
Structure of native laccase B from Trametes sp. AH28-2.,Ge H, Gao Y, Hong Y, Zhang M, Xiao Y, Teng M, Niu L Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Mar 1;66(Pt, 3):254-8. Epub 2010 Feb 23. PMID:20208154[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ge H, Gao Y, Hong Y, Zhang M, Xiao Y, Teng M, Niu L. Structure of native laccase B from Trametes sp. AH28-2. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Mar 1;66(Pt, 3):254-8. Epub 2010 Feb 23. PMID:20208154 doi:10.1107/S1744309110000084
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