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3rch

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==Crystal structure of Human aromatic L-amino acid decarboxylase (AADC) in the open conformation with LLP and PLP bound to Chain-A and Chain-B respectively==
==Crystal structure of Human aromatic L-amino acid decarboxylase (AADC) in the open conformation with LLP and PLP bound to Chain-A and Chain-B respectively==
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<StructureSection load='3rch' size='340' side='right' caption='[[3rch]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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<StructureSection load='3rch' size='340' side='right'caption='[[3rch]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3rch]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RCH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RCH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3rch]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RCH FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
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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=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rbf|3rbf]], [[3rbl|3rbl]]</td></tr>
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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;'>[[3rbf|3rbf]], [[3rbl|3rbl]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AADC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AADC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aromatic-L-amino-acid_decarboxylase Aromatic-L-amino-acid decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.28 4.1.1.28] </span></td></tr>
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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/Aromatic-L-amino-acid_decarboxylase Aromatic-L-amino-acid decarboxylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.28 4.1.1.28] </span></td></tr>
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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=3rch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rch OCA], [http://pdbe.org/3rch PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rch RCSB], [http://www.ebi.ac.uk/pdbsum/3rch PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3rch ProSAT]</span></td></tr>
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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=3rch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rch OCA], [https://pdbe.org/3rch PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rch RCSB], [https://www.ebi.ac.uk/pdbsum/3rch PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rch ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/DDC_HUMAN DDC_HUMAN]] Aromatic L-amino acid decarboxylase deficiency. The disease is caused by mutations affecting the gene represented in this entry.
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[[https://www.uniprot.org/uniprot/DDC_HUMAN DDC_HUMAN]] Aromatic L-amino acid decarboxylase deficiency. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/DDC_HUMAN DDC_HUMAN]] Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine.
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[[https://www.uniprot.org/uniprot/DDC_HUMAN DDC_HUMAN]] Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
*[[DOPA decarboxylase|DOPA decarboxylase]]
*[[DOPA decarboxylase|DOPA decarboxylase]]
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*[[User:Brian Hernandez/DOPA Decarboxylase|User:Brian Hernandez/DOPA Decarboxylase]]
 
== References ==
== References ==
<references/>
<references/>
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[[Category: Aromatic-L-amino-acid decarboxylase]]
[[Category: Aromatic-L-amino-acid decarboxylase]]
[[Category: Human]]
[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Cellini, B]]
[[Category: Cellini, B]]
[[Category: Cutruzzola, F]]
[[Category: Cutruzzola, F]]

Revision as of 05:57, 15 June 2022

Crystal structure of Human aromatic L-amino acid decarboxylase (AADC) in the open conformation with LLP and PLP bound to Chain-A and Chain-B respectively

PDB ID 3rch

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