3RCH
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
Summary for 3RCH
Entry DOI | 10.2210/pdb3rch/pdb |
Related | 3RBF 3RBL |
Descriptor | aromatic L-amino acid decarboxylase, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total) |
Functional Keywords | apo enzyme, apo form, open conformation, open dimer, exposed, conformational change, parkinson, aadc deficiency, ddc, llp, plp, decarboxylase, l-dopa, internal aldimine, shiff base, lyase |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 2 |
Total formula weight | 108401.65 |
Authors | Giardina, G.,Montioli, R.,Gianni, S.,Cellini, B.,Paiardini, A.,Borri Voltattorni, C.,Cutruzzola, F. (deposition date: 2011-03-31, release date: 2011-10-19, Last modification date: 2023-12-06) |
Primary citation | Giardina, G.,Montioli, R.,Gianni, S.,Cellini, B.,Paiardini, A.,Voltattorni, C.B.,Cutruzzola, F. Open conformation of human DOPA decarboxylase reveals the mechanism of PLP addition to Group II decarboxylases. Proc.Natl.Acad.Sci.USA, 108:20514-20519, 2011 Cited by PubMed: 22143761DOI: 10.1073/pnas.1111456108 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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