3K40
Crystal structure of Drosophila 3,4-dihydroxyphenylalanine decarboxylase
Summary for 3K40
| Entry DOI | 10.2210/pdb3k40/pdb |
| Descriptor | Aromatic-L-amino-acid decarboxylase, GLYCEROL (3 entities in total) |
| Functional Keywords | plp dependent protein, alpha beta protein, alternative splicing, catecholamine biosynthesis, decarboxylase, lyase, polymorphism, pyridoxal phosphate, cg10697-pb isoform b |
| Biological source | Drosophila melanogaster (Fruit fly) |
| Total number of polymer chains | 2 |
| Total formula weight | 107831.52 |
| Authors | Han, Q.,Ding, H.,Robinson, H.,Christensen, B.M.,Li, J. (deposition date: 2009-10-05, release date: 2010-02-02, Last modification date: 2023-11-22) |
| Primary citation | Han, Q.,Ding, H.,Robinson, H.,Christensen, B.M.,Li, J. Crystal structure and substrate specificity of Drosophila 3,4-dihydroxyphenylalanine decarboxylase Plos One, 5:e8826-e8826, 2010 Cited by PubMed Abstract: 3,4-Dihydroxyphenylalanine decarboxylase (DDC), also known as aromatic L-amino acid decarboxylase, catalyzes the decarboxylation of a number of aromatic L-amino acids. Physiologically, DDC is responsible for the production of dopamine and serotonin through the decarboxylation of 3,4-dihydroxyphenylalanine and 5-hydroxytryptophan, respectively. In insects, both dopamine and serotonin serve as classical neurotransmitters, neuromodulators, or neurohormones, and dopamine is also involved in insect cuticle formation, eggshell hardening, and immune responses. PubMed: 20098687DOI: 10.1371/journal.pone.0008826 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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