2wfl | pdb_00002wfl

Crystal structure of polyneuridine aldehyde esterase

spinqualitylabelsall models 2wfl, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wfl is a 2 chain structure with sequence from Rauvolfia serpentina. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: CME, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PNAE_RAUSE Catalyzes the hydrolysis of polyneuridine aldehyde into epi-vellosimine, which is the immediate precursor for the synthesis of the ajmaline. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structural basis and enzymatic mechanism of the biosynthesis of C9- from C10-monoterpenoid indole alkaloids.,Yang L, Hill M, Wang M, Panjikar S, Stockigt J Angew Chem Int Ed Engl. 2009;48(28):5211-3. PMID:19496101 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Polyneuridine Aldehyde Esterase

Proteopedia Page Contributors and Editors (what is this?)

OCA