1T3P | pdb_00001t3p

Half-sandwich arene ruthenium(II)-enzyme complex

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 
    0.217 (Depositor), 0.230 (DCC) 
  • R-Value Work: 
    0.182 (Depositor), 0.190 (DCC) 
  • R-Value Observed: 
    0.184 (Depositor) 

Starting Model: experimental
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Ligand Structure Quality Assessment 

Created with Raphaël 2.3.0Worse 01 BetterLigand structure goodness of fit to experimental dataBest fitted RU7Click on this verticalbar to view details

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


Literature

Half-sandwich arene ruthenium(II)-enzyme complex

McNae, I.W., Fishburne, K., Habtemariam, A., Hunter, T.M., Melchart, M., Wang, F., Walkinshaw, M.D., Sadler, P.J.

(2004) Chem Commun (Camb) 16: 1786-1787

  • DOI: https://doi.org/10.1039/b408141b
  • Primary Citation of Related Structures:  
    1T3P

  • PubMed Abstract: 

    The 1.6 [Angstrom] X-ray crystal structure of [(eta(6)-p-cymene)Ru(lysozyme)Cl(2)], the first of a half-sandwich complex of a protein, shows selective ruthenation of Nepsilon of the imidazole ring of His15.

    • Organizational Affiliation: 

    Institute of Cell and Molecular Biology, Michael Swann Building, University of Edinburgh, Mayfield Road, Edinburgh, UK.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Lysozyme C129Gallus gallusMutation(s): 0 
EC: 3.2.1.17
UniProt
Find proteins for P00698 (Gallus gallus)
Explore P00698 
Go to UniProtKB:  P00698
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00698
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free:  0.217 (Depositor), 0.230 (DCC) 
  • R-Value Work:  0.182 (Depositor), 0.190 (DCC) 
  • R-Value Observed: 0.184 (Depositor) 
Space Group: P 43 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 80.142α = 90
b = 80.142β = 90
c = 37.064γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
CCP4data scaling
MOLREPphasing

Structure Validation

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Ligand Structure Quality Assessment 

Created with Raphaël 2.3.0Worse 01 BetterLigand structure goodness of fit to experimental dataBest fitted RU7Click on this verticalbar to view details

View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-07-26
    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: 2023-08-23
    Changes: Data collection, Database references, Derived calculations, Refinement description
  • Version 1.4: 2024-10-30
    Changes: Structure summary