1CHG

CHYMOTRYPSINOGEN,2.5 ANGSTROMS CRYSTAL STRUCTURE, COMPARISON WITH ALPHA-CHYMOTRYPSIN,AND IMPLICATIONS FOR ZYMOGEN ACTIVATION


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Work: 0.430 

wwPDB Validation   3D Report Full Report


This is version 2.0 of the entry. See complete history


Literature

Chymotrypsinogen: 2.5-angstrom crystal structure, comparison with alpha-chymotrypsin, and implications for zymogen activation.

Freer, S.T.Kraut, J.Robertus, J.D.Wright, H.T.Xuong, N.H.

(1970) Biochemistry 9: 1997-2009


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CHYMOTRYPSINOGEN A245Bos taurusMutation(s): 0 
UniProt
Find proteins for P00766 (Bos taurus)
Explore P00766 
Go to UniProtKB:  P00766
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00766
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Work: 0.430 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 52α = 90
b = 63.9β = 90
c = 77.1γ = 90

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1976-11-22
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 2.0: 2023-09-27
    Type: Remediation
    Changes: Advisory, Atomic model, Data collection, Database references, Derived calculations, Other