1YS2

Burkholderia cepacia lipase complexed with hexylphosphonic acid (S) 2-methyl-3-phenylpropyl ester


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.50 Å
  • R-Value Free: 0.163 
  • R-Value Work: 0.151 
  • R-Value Observed: 0.151 

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Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

Mirror-Image Packing in Enantiomer Discrimination Molecular Basis for the Enantioselectivity of B.cepacia Lipase toward 2-Methyl-3-Phenyl-1-Propanol.

Mezzetti, A.Schrag, J.D.Cheong, C.S.Kazlauskas, R.J.

(2005) Chem Biol 12: 427-437

  • DOI: https://doi.org/10.1016/j.chembiol.2005.01.016
  • Primary Citation of Related Structures:  
    1YS1, 1YS2

  • PubMed Abstract: 

    Synthetic chemists often exploit the high enantioselectivity of lipases to prepare pure enantiomers of primary alcohols, but the molecular basis for this enantioselectivity is unknown. The crystal structures of two phosphonate transition-state analogs bound to Burkholderia cepacia lipase reveal this molecular basis for a typical primary alcohol: 2-methyl-3-phenyl-1-propanol. The enantiomeric alcohol moieties adopt surprisingly similar orientations, with only subtle differences that make it difficult to predict how to alter enantioselectivity. These structures, along with a survey of previous structures of enzyme bound enantiomers, reveal that binding of enantiomers does not involve an exchange of two substituent positions as most researchers assumed. Instead, the enantiomers adopt mirror-image packing, where three of the four substituents at the stereocenter lie in similar positions. The fourth substituent, hydrogen, points in opposite directions.


  • Organizational Affiliation

    Department of Chemistry, McGill University, Montréal, Québec H3A 2K6, Canada.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
LipaseA [auth X]320Burkholderia cepaciaMutation(s): 0 
EC: 3.1.1.3
UniProt
Find proteins for P22088 (Burkholderia cepacia)
Explore P22088 
Go to UniProtKB:  P22088
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP22088
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
2HS
Query on 2HS

Download Ideal Coordinates CCD File 
C [auth X]HEXYLPHOSPHONIC ACID (S)-2-METHYL-3-PHENYLPROPYL ESTER
C16 H27 O3 P
MMTDYBZZRYOMFD-HNNXBMFYSA-N
CA
Query on CA

Download Ideal Coordinates CCD File 
B [auth X]CALCIUM ION
Ca
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.50 Å
  • R-Value Free: 0.163 
  • R-Value Work: 0.151 
  • R-Value Observed: 0.151 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 88.93α = 90
b = 46.233β = 121.35
c = 84.729γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
CNSphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-05-17
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-08-23
    Changes: Data collection, Database references, Derived calculations, Refinement description