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3rch
From Proteopedia
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| - | [[Image:3rch.png|left|200px]] | ||
| - | + | ==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== | |
| - | + | <StructureSection load='3rch' size='340' side='right'caption='[[3rch]], [[Resolution|resolution]] 2.80Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3rch]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | |
| - | == | + | <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> |
| - | [[3rch]] is a 2 chain structure | + | </table> |
| + | == Disease == | ||
| + | [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 == | ||
| + | [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. | ||
==See Also== | ==See Also== | ||
*[[DOPA decarboxylase|DOPA decarboxylase]] | *[[DOPA decarboxylase|DOPA decarboxylase]] | ||
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | + | [[Category: Borri Voltattorni C]] | |
| - | + | [[Category: Cellini B]] | |
| - | + | [[Category: Cutruzzola F]] | |
| - | + | [[Category: Gianni S]] | |
| - | + | [[Category: Giardina G]] | |
| - | [[Category: Voltattorni | + | [[Category: Montioli R]] |
| - | [[Category: | + | [[Category: Paiardini A]] |
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Current revision
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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