1w6c: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1w6c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arthrobacter_globiformis Arthrobacter globiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W6C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W6C FirstGlance]. <br> | <table><tr><td colspan='2'>[[1w6c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arthrobacter_globiformis Arthrobacter globiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W6C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W6C FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>< | </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=NA:SODIUM+ION'>NA</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPQ:5-(2-CARBOXY-2-AMINOETHYL)-2-HYDROXY-1,4-BENZOQUINONE'>TPQ</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPQ:5-(2-CARBOXY-2-AMINOETHYL)-2-HYDROXY-1,4-BENZOQUINONE'>TPQ</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1w5z|1w5z]], [[1w6g|1w6g]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1w5z|1w5z]], [[1w6g|1w6g]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.21 and 1.4.3.22 1.4.3.21 and 1.4.3.22] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.21 and 1.4.3.22 1.4.3.21 and 1.4.3.22] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w6c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1w6c RCSB], [http://www.ebi.ac.uk/pdbsum/1w6c 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=1w6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w6c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1w6c RCSB], [http://www.ebi.ac.uk/pdbsum/1w6c PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Arthrobacter globiformis]] | [[Category: Arthrobacter globiformis]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Dooley, D M | [[Category: Dooley, D M]] | ||
[[Category: Duff, A P | [[Category: Duff, A P]] | ||
[[Category: Freeman, H C | [[Category: Freeman, H C]] | ||
[[Category: Guss, J M | [[Category: Guss, J M]] | ||
[[Category: Juda, G A | [[Category: Juda, G A]] | ||
[[Category: Langley, D B | [[Category: Langley, D B]] | ||
[[Category: Shepard, E M | [[Category: Shepard, E M]] | ||
[[Category: Amine oxidase]] | [[Category: Amine oxidase]] | ||
[[Category: Copper containing]] | [[Category: Copper containing]] | ||
[[Category: Holoenzyme]] | [[Category: Holoenzyme]] | ||
[[Category: Metal-binding]] | [[Category: Metal-binding]] | ||
[[Category: Quinone]] | [[Category: Quinone]] | ||
[[Category: Tpq]] | [[Category: Tpq]] | ||
Revision as of 17:07, 6 January 2015
AGAO holoenzyme in a small cell, at 2.2 angstromsAGAO holoenzyme in a small cell, at 2.2 angstroms
Structural highlights
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 PubMedCopper-containing amine oxidases are found in all the major kingdoms of life. They catalyse the oxidation of organic amines in the presence of molecular dioxygen to aldehydes and hydrogen peroxide. The catalytic centres contain a Cu atom and a topaquinone cofactor formed autocatalytically from a tyrosine residue in the presence of Cu and molecular oxygen. The structure of the Cu-containing amine oxidase from Arthrobacter globiformis, which was previously refined at 1.8 A resolution in space group C2 with unit-cell parameters a = 157.84, b = 63.24, c = 91.98 A, beta = 112.0 degrees [Wilce et al. (1997), Biochemistry, 36, 16116-16133], has been re-refined with newly recorded data at 1.55 A resolution. The structure has also been solved and refined at 2.2 A resolution in a new crystal form, space group C2, with unit-cell parameters a = 158.04, b = 64.06, c = 69.69 A, beta = 111.7 degrees. The copper-containing amine oxidase from Arthrobacter globiformis: refinement at 1.55 and 2.20 A resolution in two crystal forms.,Langley DB, Duff AP, Freeman HC, Guss JM Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Nov 1;62(Pt, 11):1052-7. Epub 2006 Oct 25. PMID:17077478[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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