2hkr
From Proteopedia
(Difference between revisions)
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==Structures of the carbinolamine and schiff-base intermediates in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with p-methoxyphenylethylamine== | ==Structures of the carbinolamine and schiff-base intermediates in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with p-methoxyphenylethylamine== | ||
| - | <StructureSection load='2hkr' size='340' side='right' caption='[[2hkr]], [[Resolution|resolution]] 1.40Å' scene=''> | + | <StructureSection load='2hkr' size='340' side='right'caption='[[2hkr]], [[Resolution|resolution]] 1.40Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2hkr]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2hkr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Alcfa Alcfa] and [https://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HKR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HKR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZHH:2-(4-METHOXYPHENYL)ETHANAMINE'>ZHH</scene>, <scene name='pdbligand=ZHZ:2-(4-METHOXYPHENYL)ACETAMIDE'>ZHZ</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZHH:2-(4-METHOXYPHENYL)ETHANAMINE'>ZHH</scene>, <scene name='pdbligand=ZHZ:2-(4-METHOXYPHENYL)ACETAMIDE'>ZHZ</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 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 id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2hkm|2hkm]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2hkm|2hkm]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aauB ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aauB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=511 ALCFA])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aralkylamine_dehydrogenase_(azurin) Aralkylamine dehydrogenase (azurin)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.9.2 1.4.9.2] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hkr OCA], [https://pdbe.org/2hkr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hkr RCSB], [https://www.ebi.ac.uk/pdbsum/2hkr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hkr ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://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> [[https://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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==See Also== | ==See Also== | ||
| - | *[[Aromatic amine dehydrogenase|Aromatic amine dehydrogenase]] | + | *[[Aromatic amine dehydrogenase 3D structures|Aromatic amine dehydrogenase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Alcaligenes faecalis]] | [[Category: Alcaligenes faecalis]] | ||
[[Category: Alcfa]] | [[Category: Alcfa]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Leys, D]] | [[Category: Leys, D]] | ||
[[Category: Roujeinikova, A]] | [[Category: Roujeinikova, A]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
Revision as of 07:17, 24 March 2021
Structures of the carbinolamine and schiff-base intermediates in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with p-methoxyphenylethylamine
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