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3nbj
From Proteopedia
(Difference between revisions)
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==Crystal Structure of Y305F mutant of the copper amine oxidase from Hansenula polymorpha expressed in yeast== | ==Crystal Structure of Y305F mutant of the copper amine oxidase from Hansenula polymorpha expressed in yeast== | ||
<StructureSection load='3nbj' size='340' side='right' caption='[[3nbj]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='3nbj' size='340' side='right' caption='[[3nbj]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3nbj]] is a 6 chain structure | + | <table><tr><td colspan='2'>[[3nbj]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NBJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NBJ FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ME0:HYDROXY-L-METHIONINE'>ME0</scene>, <scene name='pdbligand=TY8:2,4-BIS(HYDROPEROXY)-5-HYDROXY-L-PHENYLALANINE'>TY8</scene>, <scene name='pdbligand=TY9:3,4-BIS(HYDROPEROXY)-5-HYDROXY-L-PHENYLALANINE'>TY9</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ME0:HYDROXY-L-METHIONINE'>ME0</scene>, <scene name='pdbligand=TY8:2,4-BIS(HYDROPEROXY)-5-HYDROXY-L-PHENYLALANINE'>TY8</scene>, <scene name='pdbligand=TY9:3,4-BIS(HYDROPEROXY)-5-HYDROXY-L-PHENYLALANINE'>TY9</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a2v|1a2v]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a2v|1a2v]]</td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AMO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=870730 Ogataea angusta])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Primary-amine_oxidase Primary-amine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.21 1.4.3.21] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Primary-amine_oxidase Primary-amine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.21 1.4.3.21] </span></td></tr> | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3nbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nbj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nbj RCSB], [http://www.ebi.ac.uk/pdbsum/3nbj PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3nbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nbj OCA], [http://pdbe.org/3nbj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3nbj RCSB], [http://www.ebi.ac.uk/pdbsum/3nbj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3nbj ProSAT]</span></td></tr> |
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | + | </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=3nbj ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 3nbj" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Ogataea angusta]] | ||
[[Category: Primary-amine oxidase]] | [[Category: Primary-amine oxidase]] | ||
[[Category: Chen, Z]] | [[Category: Chen, Z]] | ||
Revision as of 07:56, 11 August 2016
Crystal Structure of Y305F mutant of the copper amine oxidase from Hansenula polymorpha expressed in yeast
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