1GCT

IS GAMMA-CHYMOTRYPSIN A TETRAPEPTIDE ACYL-ENZYME ADDUCT OF GAMMA-CHYMOTRYPSIN?

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Work: 0.173 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history. 


Literature

Is gamma-chymotrypsin a tetrapeptide acyl-enzyme adduct of alpha-chymotrypsin?

Dixon, M.M., Matthews, B.W.

(1989) Biochemistry 28: 7033-7038

  • DOI: https://doi.org/10.1021/bi00443a038
  • Primary Citation of Related Structures:  
    1GCT

  • PubMed Abstract: 

    Refinement of the structure of gamma-chymotrypsin based on X-ray crystallographic data to 1.6-A resolution has confirmed the overall conformation of the molecule as reported previously [Cohen, G. H., Silverton, E. W., & Davies, D. R. (1981) J. Mol. Biol. 148, 449-479]. In addition, the new refinement suggests that gamma-chymotrypsin, which is operationally defined by its crystalline habit, may not be the free enzyme but rather a complex, possibly an acyl-enzyme adduct, with the tetrapeptide Pro-Gly-Ala-Tyr (or a close homologue). The crystallographic refinement provides a detailed geometrical description of the enzyme-substrate-solvent interactions that occur in the presumptive adduct.

    • Organizational Affiliation: 

    Institute of Molecular Biology, University of Oregon, Eugene 97403.


Macromolecules

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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
GAMMA-CHYMOTRYPSIN A13Bos taurusMutation(s): 0 
EC: 3.4.21.1
UniProt
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Go to UniProtKB:  P00766
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UniProt GroupP00766
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
GAMMA-CHYMOTRYPSIN A131Bos taurusMutation(s): 0 
EC: 3.4.21.1
UniProt
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Go to UniProtKB:  P00766
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UniProt GroupP00766
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
GAMMA-CHYMOTRYPSIN A97Bos taurusMutation(s): 0 
EC: 3.4.21.1
UniProt
Find proteins for P00766 (Bos taurus)
Explore P00766 
Go to UniProtKB:  P00766
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UniProt GroupP00766
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  • Reference Sequence

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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
TETRAPEPTIDE ADDUCT5N/AMutation(s): 0 
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
SO4
Query on SO4
Download Ideal Coordinates CCD File 
E [auth B]SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Work: 0.173 
  • Space Group: P 42 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 69.8α = 90
b = 69.8β = 90
c = 98.1γ = 90
Software Package:
Software NamePurpose
TNTrefinement
OSCTSTdata reduction
AGROVATA/ROTAVATEdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1991-10-15
    Type: Initial release
  • Version 1.1: 2008-03-06
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2012-12-12
    Changes: Other
  • Version 1.4: 2013-03-13
    Changes: Other