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1d6u

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<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=1d6u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d6u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1d6u RCSB], [http://www.ebi.ac.uk/pdbsum/1d6u 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=1d6u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d6u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1d6u RCSB], [http://www.ebi.ac.uk/pdbsum/1d6u PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/AMO_ECOLI AMO_ECOLI]] The enzyme prefers aromatic over aliphatic amines.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 18:27, 24 December 2014

CRYSTAL STRUCTURE OF E. COLI AMINE OXIDASE ANAEROBICALLY REDUCED WITH BETA-PHENYLETHYLAMINE

1d6u, resolution 2.40Å

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