5X88

A crystal structure of cutinases from Malbranchea cinnamomea


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.76 Å
  • R-Value Free: 0.175 
  • R-Value Work: 0.172 

wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history


Literature

High-level expression and characterization of a novel cutinase from Malbranchea cinnamomea suitable for butyl butyrate production.

Duan, X.Liu, Y.You, X.Jiang, Z.Yang, S.Yang, S.

(2017) Biotechnol Biofuels 10: 223-223

  • DOI: https://doi.org/10.1186/s13068-017-0912-z
  • Primary Citation of Related Structures:  
    5X88

  • PubMed Abstract: 

    Butyl butyrate has been considered as a promising fuel source because it is a kind of natural ester which can be converted from renewable and sustainable lignocellulosic biomass. Compared with the conventional chemical methods for butyl butyrate production, the enzymatic approach has been demonstrated to be more attractive, mainly owing to the mild reaction conditions, high specificity, low energy consumption, and environmental friendliness. Cutinases play an important role in the butyl butyrate production process. However, the production level of cutinases is still relatively low. Thus, to identify novel cutinases suitable for butyl butyrate synthesis and enhance their yields is of great value in biofuel industry.


  • Organizational Affiliation

    Beijing Advanced Innovation Center for Food Nutrition and Human Health, China Agricultural University, Beijing, 100083 China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
cutinase199Malbranchea cinnamomeaMutation(s): 0 
EC: 3.1.1.74
UniProt
Find proteins for A0A1S6YJF3 (Malbranchea cinnamomea)
Explore A0A1S6YJF3 
Go to UniProtKB:  A0A1S6YJF3
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A1S6YJF3
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.76 Å
  • R-Value Free: 0.175 
  • R-Value Work: 0.172 
  • Space Group: P 21 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 34.407α = 90
b = 37.815β = 90
c = 127.967γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling
PHENIXphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2018-01-31
    Type: Initial release