3rbl
From Proteopedia
(Difference between revisions)
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==Crystal structure of Human aromatic L-amino acid decarboxylase (AADC) in the apo form== | ==Crystal structure of Human aromatic L-amino acid decarboxylase (AADC) in the apo form== | ||
- | <StructureSection load='3rbl' size='340' side='right' caption='[[3rbl]], [[Resolution|resolution]] 3.24Å' scene=''> | + | <StructureSection load='3rbl' size='340' side='right'caption='[[3rbl]], [[Resolution|resolution]] 3.24Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3rbl]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3rbl]] 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=3RBL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RBL FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rbf|3rbf]], [[3rch|3rch]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3rbf|3rbf]], [[3rch|3rch]]</div></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AADC ([ | + | <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> |
- | <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/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> |
- | <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=3rbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rbl OCA], [https://pdbe.org/3rbl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rbl RCSB], [https://www.ebi.ac.uk/pdbsum/3rbl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rbl ProSAT]</span></td></tr> |
</table> | </table> | ||
== Disease == | == 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 == | == 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. |
<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]] | ||
- | *[[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]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: Cellini, B]] | [[Category: Cellini, B]] | ||
[[Category: Cutruzzola, F]] | [[Category: Cutruzzola, F]] |
Revision as of 05:56, 15 June 2022
Crystal structure of Human aromatic L-amino acid decarboxylase (AADC) in the apo form
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Categories: Aromatic-L-amino-acid decarboxylase | Human | Large Structures | Cellini, B | Cutruzzola, F | Gianni, S | Giardina, G | Montioli, R | Paiardini, A | Voltattorni, C Borri | Aadc deficiency | Apo enzyme | Apo form | Conformational change | Ddc | Decarboxylase | Exposed | L-dopa | Lyase | Open conformation | Open dimer | Parkinson | Plp