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2wgq
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2wgq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WGQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WGQ FirstGlance]. <br> | <table><tr><td colspan='2'>[[2wgq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WGQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WGQ 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=ZN:ZINC+ION'>ZN</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dyu|1dyu]], [[1oac|1oac]], [[1qak|1qak]], [[1qal|1qal]], [[1d6u|1d6u]], [[1jrq|1jrq]], [[1spu|1spu]], [[2w0q|2w0q]], [[1qaf|1qaf]], [[1d6y|1d6y]], [[1d6z|1d6z]], [[1lvn|1lvn]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dyu|1dyu]], [[1oac|1oac]], [[1qak|1qak]], [[1qal|1qal]], [[1d6u|1d6u]], [[1jrq|1jrq]], [[1spu|1spu]], [[2w0q|2w0q]], [[1qaf|1qaf]], [[1d6y|1d6y]], [[1d6z|1d6z]], [[1lvn|1lvn]]</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=2wgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wgq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wgq RCSB], [http://www.ebi.ac.uk/pdbsum/2wgq 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=2wgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wgq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wgq RCSB], [http://www.ebi.ac.uk/pdbsum/2wgq PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[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]] | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
| - | [[Category: Cooper, R A | + | [[Category: Cooper, R A]] |
| - | [[Category: Moody, P C.E | + | [[Category: Moody, P C.E]] |
[[Category: Amine oxidase]] | [[Category: Amine oxidase]] | ||
[[Category: Metal-binding]] | [[Category: Metal-binding]] | ||
| - | [[Category: Oxidoreductase]] | ||
[[Category: Tpq]] | [[Category: Tpq]] | ||
Revision as of 00:00, 25 December 2014
ZINC SUBSTITUTED E COLI COPPER AMINE OXIDASE, A MODEL FOR THE PRECURSOR FOR 2,4,5-TRIHYDROXYPHENYLALANINEQUINONE FORMATION
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