1FCS

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

Summary for 1FCS

• Entry DOI: 10.2210/pdb1fcs/pdb
• Descriptor: MYOGLOBIN, SULFATE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• Functional Keywords: oxygen transport
• Biological source: Physeter catodon (sperm whale)
• Total number of polymer chains: 1
• Total formula weight: 18190.85

Authors

Rizzi, M.,Bolognesi, M.,Coda, A.,Cutruzzola, F.,Travaglini Allocatelli, C.,Brancaccio, A.,Brunori, M. (deposition date: 1993-04-20, release date: 1993-10-31, Last modification date: 2024-02-07)

Primary citation

Rizzi, M.,Bolognesi, M.,Coda, A.,Cutruzzola, F.,Allocatelli, C.T.,Brancaccio, A.,Brunori, M.
Crystal structure of a distal site double mutant of sperm whale myoglobin at 1.6 A resolution.
FEBS Lett., 320:13-16, 1993

PubMed 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.

PubMed: 8462669
DOI: 10.1016/0014-5793(93)81647-I

Experimental method

X-RAY DIFFRACTION (1.6 Å)