3GZJ

Crystal Structure of Polyneuridine Aldehyde Esterase Complexed with 16-epi-Vellosimine

Summary for 3GZJ

Entry DOI	10.2210/pdb3gzj/pdb
Descriptor	Polyneuridine-aldehyde esterase, 16-epi-Vellosimine (3 entities in total)
Functional Keywords	hydrolase superfamily, alkaloid metabolism, hydrolase, serine esterase
Biological source	Rauvolfia serpentina (devilpepper)
Total number of polymer chains	5
Total formula weight	146227.65
Authors	Yang, L.,Hill, M.,Wang, M.,Panjikar, S.,Stoeckigt, J. (deposition date: 2009-04-07, release date: 2009-08-18, Last modification date: 2023-11-01)
Primary citation	Yang, L.,Hill, M.,Wang, M.,Panjikar, S.,Stockigt, J. Structural basis and enzymatic mechanism of the biosynthesis of C9- from C10-monoterpenoid indole alkaloids Angew.Chem.Int.Ed.Engl., 48:5211-5213, 2009 Cited by PubMed Abstract: Cutting carbons: The three-dimensional structure of polyneuridine aldehyde esterase (PNAE) gives insight into the enzymatic mechanism of the biosynthesis of C(9)- from C(10)-monoterpenoid indole alkaloids (see scheme). PNAE is a very substrate-specific serine esterase. It harbors the catalytic triad S87-D216-H244, and is a new member of the alpha/beta-fold hydrolase superfamily. Its novel function leads to the diversification of alkaloid structures. PubMed: 19496101 DOI: 10.1002/anie.200900150 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.19 Å)

Structure validation