5M0Z

Cyclohexanone Monooxygenase from T. municipale: reduced enzyme bound to NADP+


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.177 
  • R-Value Work: 0.148 
  • R-Value Observed: 0.149 

Starting Model: experimental
View more details

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 2.1 of the entry. See complete history


Literature

Characterization and Crystal Structure of a Robust Cyclohexanone Monooxygenase.

Romero, E.Castellanos, J.R.Mattevi, A.Fraaije, M.W.

(2016) Angew Chem Int Ed Engl 55: 15852-15855

  • DOI: https://doi.org/10.1002/anie.201608951
  • Primary Citation of Related Structures:  
    5M0Z, 5M10

  • PubMed Abstract: 

    Cyclohexanone monooxygenase (CHMO) is a promising biocatalyst for industrial reactions owing to its broad substrate spectrum and excellent regio-, chemo-, and enantioselectivity. However, the low stability of many Baeyer-Villiger monooxygenases is an obstacle for their exploitation in industry. Characterization and crystal structure determination of a robust CHMO from Thermocrispum municipale is reported. The enzyme efficiently converts a variety of aliphatic, aromatic, and cyclic ketones, as well as prochiral sulfides. A compact substrate-binding cavity explains its preference for small rather than bulky substrates. Small-scale conversions with either purified enzyme or whole cells demonstrated the remarkable properties of this newly discovered CHMO. The exceptional solvent tolerance and thermostability make the enzyme very attractive for biotechnology.


  • Organizational Affiliation

    Department of Biotechnology, University of Groningen, Nijenborgh 4, 9747AG, Groningen, The Netherlands.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Cyclohexanone Monooxygenase from Thermocrispum municipale.541Thermocrispum municipale DSM 44069Mutation(s): 0 
EC: 1.14.13.22
UniProt
Find proteins for A0A1L1QK39 (Thermocrispum municipale DSM 44069)
Explore A0A1L1QK39 
Go to UniProtKB:  A0A1L1QK39
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A1L1QK39
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Experimental Data & Validation

Experimental Data

Unit Cell:
Length ( Å )Angle ( ˚ )
a = 69.206α = 90
b = 114.677β = 90
c = 155.435γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
EU Horizon 2020 Programme Research and Innovation actions H2020-LEIT BIO-2014-1635734

Revision History  (Full details and data files)

  • Version 1.0: 2016-12-07
    Type: Initial release
  • Version 1.1: 2016-12-21
    Changes: Database references
  • Version 2.0: 2020-04-22
    Changes: Atomic model, Database references
  • Version 2.1: 2024-01-17
    Changes: Data collection, Database references, Refinement description