2HMZ: The Structures Of Met And Azidomet Hemerythrin At 1.66 Angstroms Resolution

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.
PDB ID: 2HMZDownload
MMDB ID: 2721
PDB Deposition Date: 1990/10/18
Updated in MMDB: 2012/12
Experimental Method:
x-ray diffraction
Resolution: 1.66  Å
Source Organism:
Similar Structures:
Biological Unit for 2HMZ: octameric; determined by author and by software (PISA,PQS)
Molecular Components in 2HMZ
Label Count Molecule
Proteins (8 molecules)
Molecule annotation
Chemicals (16 molecules)
* Click molecule labels to explore molecular sequence information.

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