2GCH

REFINED CRYSTAL STRUCTURE OF GAMMA-CHYMOTRYPSIN AT 1.9 ANGSTROMS RESOLUTION

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Work: 0.181 

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This is version 1.2 of the entry. See complete history. 


Literature

Refined crystal structure of gamma-chymotrypsin at 1.9 A resolution. Comparison with other pancreatic serine proteases.

Cohen, G.H., Silverton, E.W., Davies, D.R.

(1981) J Mol Biol 148: 449-479


Macromolecules

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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
GAMMA-CHYMOTRYPSIN AA [auth E]13Bos taurusMutation(s): 0 
EC: 3.4.21.1
UniProt
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UniProt GroupP00766
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
GAMMA-CHYMOTRYPSIN AB [auth F]131Bos taurusMutation(s): 0 
EC: 3.4.21.1
UniProt
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
GAMMA-CHYMOTRYPSIN AC [auth G]97Bos taurusMutation(s): 0 
EC: 3.4.21.1
UniProt
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Explore P00766 
Go to UniProtKB:  P00766
Entity Groups  
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UniProt GroupP00766
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Work: 0.181 
  • Space Group: P 42 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 69.6α = 90
b = 69.6β = 90
c = 97.4γ = 90
Software Package:
Software NamePurpose
PROLSQrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1980-07-09
    Type: Initial release
  • Version 1.1: 2008-03-03
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance