2HMZ

THE STRUCTURES OF MET AND AZIDOMET HEMERYTHRIN AT 1.66 ANGSTROMS RESOLUTION


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.66 Å
  • R-Value Observed: 0.176 

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This is version 1.2 of the entry. See complete history


Literature

Structures of met and azidomet hemerythrin at 1.66 A resolution.

Holmes, M.A.Stenkamp, R.E.

(1991) J Mol Biol 220: 723-737

  • DOI: https://doi.org/10.1016/0022-2836(91)90113-k
  • Primary Citation of Related Structures:  
    2HMQ, 2HMZ

  • PubMed Abstract: 

    The crystallographic refinement of met and azidomet hemerythrin has been carried out at 1.66 A resolution in an attempt to characterize precisely the binuclear iron center in this protein. Restrained least-squares refinement has produced molecular models giving R-values of 18.9% for met (65,683 reflections from 10 A to 1.66 A) and 17.6% for azidomet hemerythrin (68,747 reflections from 10.0 A to 1.66 A). The protein structure in each derivative is very similar to that of myohemerythrin. The mu-oxo bridged iron center differs between the two forms. The complex in met hemerythrin is asymmetric with the bridging oxygen closer to one of the iron atoms while the complex in azidomet hemerythrin is symmetric. After investigations of the effects of correlation in the refinement, we believe this difference between the two complexes is associated with chemical differences and is not a refinement artefact.


  • Organizational Affiliation

    Department of Biological Structure, University of Washington, Seattle 98195.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
HEMERYTHRIN
A, B, C, D
113Themiste dyscritumMutation(s): 1 
UniProt
Find proteins for P02246 (Themiste dyscrita)
Explore P02246 
Go to UniProtKB:  P02246
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP02246
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.66 Å
  • R-Value Observed: 0.176 
  • Space Group: P 4
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 86.6α = 90
b = 86.6β = 90
c = 80.8γ = 90
Software Package:
Software NamePurpose
PROFFTrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1992-01-15
    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