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2hkm

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(New page: 200px {{Structure |PDB= 2hkm |SIZE=350|CAPTION= <scene name='initialview01'>2hkm</scene>, resolution 1.500&Aring; |SITE= <scene name='pdbsite=AC1:Pea+Binding+Site...)
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[[Image:2hkm.jpg|left|200px]]
 
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{{Structure
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==Crystal structure of the Schiff base intermediate in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with phenylethylamine.==
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|PDB= 2hkm |SIZE=350|CAPTION= <scene name='initialview01'>2hkm</scene>, resolution 1.500&Aring;
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<StructureSection load='2hkm' size='340' side='right'caption='[[2hkm]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Pea+Binding+Site+For+Residue+H+1401'>AC1</scene> and <scene name='pdbsite=AC2:Pea+Binding+Site+For+Residue+D+1402'>AC2</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=PEA:2-PHENYLETHYLAMINE'>PEA</scene>, <scene name='pdbligand=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</scene>
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<table><tr><td colspan='2'>[[2hkm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HKM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HKM FirstGlance]. <br>
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|ACTIVITY= <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>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEA:2-PHENYLETHYLAMINE'>PEA</scene></td></tr>
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|GENE=
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<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>
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|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam02975 Me-amine-dh_L], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam06433 Me-amine-dh_H]</span>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2hj4|2hj4]], [[2hj7|2hj7]], [[2hjb|2hjb]], [[2hkr|2hkr]]</div></td></tr>
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|RELATEDENTRY=[[2hj4|2HJ4]], [[2hj7|2HJ7]], [[2hjb|2HJB]], [[2hkr|2HKR]]
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<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>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hkm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hkm OCA], [http://www.ebi.ac.uk/pdbsum/2hkm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hkm RCSB]</span>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hkm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hkm OCA], [https://pdbe.org/2hkm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hkm RCSB], [https://www.ebi.ac.uk/pdbsum/2hkm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hkm ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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[[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hk/2hkm_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/main_output.php?pdb_ID=2hkm ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of the Schiff base intermediate in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with phenylethylamine.'''
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==See Also==
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*[[Aromatic amine dehydrogenase 3D structures|Aromatic amine dehydrogenase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HKM OCA].
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__TOC__
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[[Category: Aralkylamine dehydrogenase]]
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</StructureSection>
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[[Category: Leys, D.]]
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[[Category: Alcaligenes faecalis]]
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[[Category: Roujeinikova, A.]]
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[[Category: Large Structures]]
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[[Category: oxidoreductase]]
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[[Category: Leys, D]]
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[[Category: Roujeinikova, A]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 2 11:57:14 2008''
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[[Category: Oxidoreductase]]

Current revision

Crystal structure of the Schiff base intermediate in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with phenylethylamine.

PDB ID 2hkm

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