2EA3

Crystal Structure Of Cellulomonas Bogoriensis Chymotrypsin


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.78 Å
  • R-Value Free: 0.195 
  • R-Value Work: 0.166 
  • R-Value Observed: 0.167 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structure determination and analysis of a bacterial chymotrypsin from Cellulomonas bogoriensis

Shaw, A.Saldajeno, M.L.Kolkman, M.A.Jones, B.E.Bott, R.

(2007) Acta Crystallogr Sect F Struct Biol Cryst Commun 63: 266-269

  • DOI: https://doi.org/10.1107/S1744309107008937
  • Primary Citation of Related Structures:  
    2EA3

  • PubMed Abstract: 

    The crystal structure of a secreted chymotrypsin from the alkaliphile Cellulomonas bogoriensis has been determined using data to 1.78 A resolution and refined to a crystallographic R factor of 0.167. The crystal structure reveals a large P1 substrate-specificity pocket, as expected for chymotrypsins. The structure is compared with close structural homologues. This comparison does not reveal clear reasons for the alkali tolerance of the enzyme, but the greater compactness of the structure and lowered hydrogen bonding may play a role.


  • Organizational Affiliation

    Genencor, Palo Alto, CA 94304, USA. andy.shaw@danisco.com


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Chymotrypsin189Cellulomonas bogoriensisMutation(s): 0 
EC: 3.4.21
UniProt
Find proteins for A2RQE2 (Cellulomonas bogoriensis)
Explore A2RQE2 
Go to UniProtKB:  A2RQE2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA2RQE2
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.78 Å
  • R-Value Free: 0.195 
  • R-Value Work: 0.166 
  • R-Value Observed: 0.167 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 36.19α = 90
b = 52.49β = 90
c = 76.63γ = 90
Software Package:
Software NamePurpose
REFMACrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-04-24
    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: 2023-10-25
    Changes: Data collection, Database references, Derived calculations, Refinement description