4GCH

STRUCTURE AND ACTIVITY OF TWO PHOTOREVERSIBLE CINNAMATES BOUND TO CHYMOTRYPSIN


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Observed: 0.209 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structure and activity of two photoreversible cinnamates bound to chymotrypsin.

Stoddard, B.L.Bruhnke, J.Porter, N.Ringe, D.Petsko, G.A.

(1990) Biochemistry 29: 4871-4879

  • DOI: https://doi.org/10.1021/bi00472a017
  • Primary Citation of Related Structures:  
    3GCH, 4GCH

  • PubMed Abstract: 

    The serine protease gamma-chymotrypsin was covalently inhibited with two different photoreversible cinnamate compounds, and the structures of the resulting complexes were determined to 1.9-A resolution. The inhibitors show different kinetics of binding, inhibition, and nonphotochemical deacylation relative to each other in solution activity assays. The crystal structures of the enzyme-cinnamate complexes show that both compounds acylate serine 195 and that the two molecules are bound in similar nonproductive conformations which have drastic effects on their ability to turn over. Substitution of a diethylamino group on the para position of the cinnamate ring causes a 1000-fold increase in the thermal stability of the inhibitor toward hydrolysis and deacylation.


  • Organizational Affiliation

    Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139.


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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Go to UniProtKB:  P00766
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UniProt GroupP00766
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  • Reference Sequence
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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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Explore P00766 
Go to UniProtKB:  P00766
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UniProt GroupP00766
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  • Reference Sequence
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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
Find proteins for P00766 (Bos taurus)
Explore P00766 
Go to UniProtKB:  P00766
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00766
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
DMC
Query on DMC

Download Ideal Coordinates CCD File 
D [auth G]3-(4-DIETHYLAMINO-2-HYDROXY-PHENYL)-2-METHYL-PROPIONIC ACID
C14 H19 N O3
JAEWDFYDSACHDN-CSKARUKUSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Observed: 0.209 
  • Space Group: P 42 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 69.7α = 90
b = 69.7β = 90
c = 97.5γ = 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: 1990-10-15
    Type: Initial release
  • Version 1.1: 2008-03-25
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance