2agy
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2agy]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AGY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AGY FirstGlance]. <br> | <table><tr><td colspan='2'>[[2agy]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AGY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AGY FirstGlance]. <br> | ||
- | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TSH:2-(1H-INDOL-3-YL)ETHANIMINE'>TSH</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TSH:2-(1H-INDOL-3-YL)ETHANIMINE'>TSH</scene></td></tr> |
- | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</scene></td></tr> | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</scene></td></tr> |
- | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2agl|2agl]], [[2agu|2agu]], [[2agw|2agw]], [[2agx|2agx]], [[2agz|2agz]], [[2ah0|2ah0]], [[2ah1|2ah1]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2agl|2agl]], [[2agu|2agu]], [[2agw|2agw]], [[2agx|2agx]], [[2agz|2agz]], [[2ah0|2ah0]], [[2ah1|2ah1]]</td></tr> |
- | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aralkylamine_dehydrogenase Aralkylamine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.99.4 1.4.99.4] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aralkylamine_dehydrogenase Aralkylamine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.99.4 1.4.99.4] </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=2agy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2agy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2agy RCSB], [http://www.ebi.ac.uk/pdbsum/2agy 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=2agy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2agy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2agy RCSB], [http://www.ebi.ac.uk/pdbsum/2agy PDBsum]</span></td></tr> |
- | <table> | + | </table> |
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/AAUA_ALCFA AAUA_ALCFA]] Oxidizes primary aromatic amines and, more slowly, some long-chain aliphatic amines, but not methylamine or ethylamine. Uses azurin as an electron acceptor to transfer electrons from the reduced tryptophylquinone cofactor.<ref>PMID:11495996</ref> <ref>PMID:16279953</ref> <ref>PMID:8188594</ref> <ref>PMID:7876189</ref> <ref>PMID:17087503</ref> <ref>PMID:17005560</ref> <ref>PMID:16614214</ref> [[http://www.uniprot.org/uniprot/AAUB_ALCFA AAUB_ALCFA]] Oxidizes primary aromatic amines and, more slowly, some long-chain aliphatic amines, but not methylamine or ethylamine. Uses azurin as an electron acceptor to transfer electrons from the reduced tryptophylquinone cofactor.<ref>PMID:11495996</ref> <ref>PMID:16279953</ref> <ref>PMID:8188594</ref> <ref>PMID:16614214</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Alcaligenes faecalis]] | [[Category: Alcaligenes faecalis]] | ||
[[Category: Aralkylamine dehydrogenase]] | [[Category: Aralkylamine dehydrogenase]] | ||
- | [[Category: Basran, J | + | [[Category: Basran, J]] |
- | [[Category: Hothi, P | + | [[Category: Hothi, P]] |
- | [[Category: Johannissen, L O | + | [[Category: Johannissen, L O]] |
- | [[Category: Leys, D | + | [[Category: Leys, D]] |
- | [[Category: Masgrau, L | + | [[Category: Masgrau, L]] |
- | [[Category: Mulholland, A J | + | [[Category: Mulholland, A J]] |
- | [[Category: Ranaghan, K E | + | [[Category: Ranaghan, K E]] |
- | [[Category: Roujeinikova, A | + | [[Category: Roujeinikova, A]] |
- | [[Category: Scrutton, N S | + | [[Category: Scrutton, N S]] |
- | [[Category: Sutcliffe, M J | + | [[Category: Sutcliffe, M J]] |
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] |
Revision as of 19:35, 25 December 2014
Crystal structure of the Schiff base intermediate in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with tryptamine. Monoclinic form
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