View source for 3wa3


==Crystal structure of copper amine oxidase from arthrobacter globiformis in N2 condition==
<StructureSection load='3wa3' size='340' side='right'caption='[[3wa3]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wa3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"achromobacter_globiformis"_(conn_1928)_bergey_et_al._1930 "achromobacter globiformis" (conn 1928) bergey et al. 1930]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WA3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WA3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HDZ:NITROGEN+MOLECULE'>HDZ</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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 id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3wa2|3wa2]]</div></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Primary-amine_oxidase Primary-amine oxidase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3wa3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wa3 OCA], [https://pdbe.org/3wa3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wa3 RCSB], [https://www.ebi.ac.uk/pdbsum/3wa3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wa3 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of a copper amine oxidase from Arthrobacter globiformis was determined at 1.08 A resolution with the use of low-molecular-weight polyethylene glycol (LMW PEG; average molecular weight approximately 200) as a cryoprotectant. The final crystallographic R factor and Rfree were 13.0 and 15.0%, respectively. Several molecules of LMW PEG were found to occupy cavities in the protein interior, including the active site, which resulted in a marked reduction in the overall B factor and consequently led to a subatomic resolution structure for a relatively large protein with a monomer molecular weight of approximately 70 000. About 40% of the presumed H atoms were observed as clear electron densities in the Fo - Fc difference map. Multiple minor conformers were also identified for many residues. Anisotropic displacement fluctuations were evaluated in the active site, which contains a post-translationally derived quinone cofactor and a Cu atom. Furthermore, diatomic molecules, most likely to be molecular oxygen, are bound to the protein, one of which is located in a region that had previously been proposed as an entry route for the dioxygen substrate from the central cavity of the dimer interface to the active site.

High-resolution crystal structure of copper amine oxidase from Arthrobacter globiformis: assignment of bound diatomic molecules as O2.,Murakawa T, Hayashi H, Sunami T, Kurihara K, Tamada T, Kuroki R, Suzuki M, Tanizawa K, Okajima T Acta Crystallogr D Biol Crystallogr. 2013 Dec;69(Pt 12):2483-94. doi:, 10.1107/S0907444913023196. Epub 2013 Nov 19. PMID:24311589<ref>PMID:24311589</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wa3" style="background-color:#fffaf0;"></div>

==See Also==
*[[Copper amine oxidase 3D structures|Copper amine oxidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Primary-amine oxidase]]
[[Category: Hayashi, H]]
[[Category: Kurihara, K]]
[[Category: Kuroki, R]]
[[Category: Murakawa, T]]
[[Category: Okajima, T]]
[[Category: Sunami, T]]
[[Category: Suzuki, M]]
[[Category: Tamada, T]]
[[Category: Tanizawa, K]]
[[Category: Copper binding]]
[[Category: Cytoplassm]]
[[Category: Oxidase]]
[[Category: Oxidoreductase]]
[[Category: Post-translationally derived quinone cofactor]]