1fcs

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Image:1fcs.gif

1fcs, resolution 1.6Å

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CRYSTAL STRUCTURE OF A DISTAL SITE DOUBLE MUTANT OF SPERM WHALE MYOGLOBIN AT 1.6 ANGSTROMS RESOLUTION

Overview

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.

About this Structure

1FCS is a Single protein structure of sequence from Physeter catodon with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of a distal site double mutant of sperm whale myoglobin at 1.6 A resolution., Rizzi M, Bolognesi M, Coda A, Cutruzzola F, Allocatelli CT, Brancaccio A, Brunori M, FEBS Lett. 1993 Mar 29;320(1):13-6. PMID:8462669

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