1HBI

CRYSTAL STRUCTURE OF OXYGENATED SCAPHARCA DIMERIC HEMOGLOBIN AT 1.7 ANGSTROMS RESOLUTION

Summary for 1HBI

• Entry DOI: 10.2210/pdb1hbi/pdb
• Descriptor: HEMOGLOBIN (OXY), PROTOPORPHYRIN IX CONTAINING FE, OXYGEN MOLECULE, ... (4 entities in total)
• Functional Keywords: oxygen transport
• Biological source: Scapharca inaequivalvis (ark clam)
• Total number of polymer chains: 2
• Total formula weight: 33229.61

Authors

Royer Junior, W.E.,Condon, P.J. (deposition date: 1994-06-22, release date: 1994-10-15, Last modification date: 2024-02-07)

Primary citation

Condon, P.J.,Royer Jr., W.E.
Crystal structure of oxygenated Scapharca dimeric hemoglobin at 1.7-A resolution.
J.Biol.Chem., 269:25259-25267, 1994

PubMed Abstract: The crystal structure of the cooperative dimeric hemoglobin from the blood clam Scapharca inaequivalvis has been determined in the oxygenated state and refined to an R-factor of 0.157 at 1.7-A resolution. The structure is very similar to the carbon monoxide-liganded form with subtle differences in ligand binding geometry. Oxygen binds to the heme iron in a bent conformation with Fe-O-O angles of 135 degrees and 150 degrees for the two subunits. These observed angles are lower than the equivalent angles in the carbon monoxide-liganded form and intermediate between the angles observed in structures of oxygenated sperm whale myoglobin and oxygenated human hemoglobin. This third high resolution structure of Scapharca dimeric hemoglobin permits a detailed analysis of the water structure in the highly hydrated interface between subunits.

PubMed: 7929217

Experimental method

X-RAY DIFFRACTION (1.7 Å)