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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 DOI10.2210/pdb3rch/pdb
Related3RBF 3RBL
Descriptoraromatic L-amino acid decarboxylase, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total)
Functional Keywordsapo 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 sourceHomo sapiens (human)
More
Total number of polymer chains2
Total formula weight108401.65
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 citationGiardina, 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: 22143761
DOI: 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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