3k5t
From Proteopedia
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| - | [[  | + | ==Crystal structure of human diamine oxidase in space group C2221==  | 
| + | <StructureSection load='3k5t' size='340' side='right' caption='[[3k5t]], [[Resolution|resolution]] 2.11Å' scene=''>  | ||
| + | == Structural highlights ==  | ||
| + | <table><tr><td colspan='2'>[[3k5t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K5T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3K5T FirstGlance]. <br>  | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>  | ||
| + | <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><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABP1, AOC1, DAO1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>  | ||
| + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Diamine_oxidase Diamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.22 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=3k5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k5t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3k5t RCSB], [http://www.ebi.ac.uk/pdbsum/3k5t PDBsum]</span></td></tr>  | ||
| + | <table>  | ||
| + | == 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/k5/3k5t_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/chain_selection.php?pdb_ID=2ata ConSurf].  | ||
| + | <div style="clear:both"></div>  | ||
| + | <div style="background-color:#fffaf0;">  | ||
| + | == Publication Abstract from PubMed ==  | ||
| + | Copper amine oxidases (CAOs) are ubiquitous in nature and catalyse the oxidative deamination of primary amines to the corresponding aldehydes. Humans have three viable CAO genes (AOC1-3). AOC1 encodes human diamine oxidase (hDAO), which is the frontline enzyme for histamine metabolism. hDAO is unique among CAOs in that it has a distinct substrate preference for diamines. The structure of hDAO in space group P2(1)2(1)2(1) with two molecules in the asymmetric unit has recently been reported. Here, the structure of hDAO refined to 2.1 A resolution in space group C222(1) with one molecule in the asymmetric unit is reported.  | ||
| - | + | A new crystal form of human diamine oxidase.,McGrath AP, Hilmer KM, Collyer CA, Dooley DM, Guss JM Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Feb 1;66(Pt 2):137-42., Epub 2010 Jan 27. PMID:20124708<ref>PMID:20124708</ref>  | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>  | |
| - | + | </div>  | |
| - | + | == References ==  | |
| - | + | <references/>  | |
| - | + | __TOC__  | |
| - | + | </StructureSection>  | |
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| - | ==  | + | |
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[[Category: Diamine oxidase]]  | [[Category: Diamine oxidase]]  | ||
[[Category: Homo sapiens]]  | [[Category: Homo sapiens]]  | ||
Revision as of 09:43, 21 May 2014
Crystal structure of human diamine oxidase in space group C2221
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Categories: Diamine oxidase | Homo sapiens | Guss, J M. | McGrath, A P. | Cao | Copper amine oxidase | Dao | Glycoprotein | Heparin-binding | Human | Metal-binding | Oxidoreductase | Secreted | Topaquinone | Tpq

