| Myohemerythrin | |
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Cartoons view of Myohemerythrin, a 4-helix bundle. N-terminus is colored blue, C-terminus is red.
All helices are anti-parallel with respect to their 2 nearest neighbors.
Myohemerythrin binds Oxygen (Red) by using 2 Fe ions (Orange). This binding site is found between the helices.
The Fe ions are chelated by the amino acid side chains: 1 Asp, 1 Glu and 5 His.
The side chains are tightly packed against each other. Also the N-terminus wraps around the C-terminal helix, which gives the protein a more globular structure.
Structure of myohemerythrin in the azidomet state at 1.7/1.3 A resolution. Sheriff, S., Hendrickson, W.A., Smith, J.L., (1987) J.Mol.Biol. 197: 273-296 (PubMed) 2mhr(PDB) |