2WFM

Crystal structure of polyneuridine aldehyde esterase mutant (H244A)

Summary for 2WFM

Entry DOI	10.2210/pdb2wfm/pdb
Related	2WFL
Descriptor	POLYNEURIDINE ALDEHYDE ESTERASE (2 entities in total)
Functional Keywords	alkaloid metabolism, monoterpenoid indole alkaloids, pnae, hydrolase, serine esterase
Biological source	RAUVOLFIA SERPENTINA (SERPENTWOOD)
Total number of polymer chains	5
Total formula weight	148121.49
Authors	Yang, L.,Hill, M.,Panjikar, S.,Wang, M.,Stoeckigt, J. (deposition date: 2009-04-08, release date: 2010-04-21, Last modification date: 2023-12-13)
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-, 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 (2.2 Å)

Structure validation