2WFM

Crystal structure of polyneuridine aldehyde esterase mutant (H244A)

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.236 
  • R-Value Work: 0.198 
  • R-Value Observed: 0.198 

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This is version 1.2 of the entry. See complete history. 


Literature

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.

(2009) Angew Chem Int Ed Engl 48: 5211

  • DOI: https://doi.org/10.1002/anie.200900150
  • Primary Citation of Related Structures:  
    2WFL, 2WFM, 3GZJ

  • 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.

    • Organizational Affiliation: 

    Institute of Materia Medica, College of Pharmaceutical Sciences, Zhejiang University, 383 Yu Hang Tang Road, Hangzhou 310058, China.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
POLYNEURIDINE ALDEHYDE ESTERASE
A, B, C, D, E
264Rauvolfia serpentinaMutation(s): 1 
EC: 3.1.1.78
UniProt
Find proteins for Q9SE93 (Rauvolfia serpentina)
Explore Q9SE93 
Go to UniProtKB:  Q9SE93
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9SE93
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.236 
  • R-Value Work: 0.198 
  • R-Value Observed: 0.198 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 170.25α = 90
b = 46.81β = 104.89
c = 184.17γ = 90
Software Package:
Software NamePurpose
XDSdata reduction
XSCALEdata scaling
Auto-Rickshawphasing
MOLREPphasing
REFMACrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-04-21
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.2: 2023-12-13
    Changes: Data collection, Database references, Other, Refinement description