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. 1993 Mar 29;320(1):13-6.
doi: 10.1016/0014-5793(93)81647-i.

Crystal structure of a distal site double mutant of sperm whale myoglobin at 1.6 A resolution

M Rizzi  1 , M Bolognesi, A Coda, F Cutruzzolà, C T Allocatelli, A Brancaccio, M Brunori
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Free article

Crystal structure of a distal site double mutant of sperm whale myoglobin at 1.6 A resolution

M Rizzi et al. FEBS Lett. .
Free article

Abstract

The three-dimensional structure of sperm whale myoglobin His64(E7)-->Val,Thr67(E10)-->Arg double mutant has been studied by X-ray crystallography at 1.6 A resolution, and refined to a crystallographic R-factor of 0.197. The Arg67(E10) side chain is extended in the direction of the ligand binding site, and its NH1 atom is at a distance of 3.11 A from the NH1 atom of Arg45(CD3), which is also pointing towards the distal site. Both are kept in this position by hydrogen bonding and electrostatic interactions with a solvent sulfate ion, located amongst the two, on the protein surface. No liganded water molecule is present at the sixth coordination position of the Fe(III) heme.

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