1hbi
CRYSTAL STRUCTURE OF OXYGENATED SCAPHARCA DIMERIC HEMOGLOBIN AT 1.7 ANGSTROMS RESOLUTION
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| , resolution 1.7Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
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.
About this StructureAbout this Structure
1HBI is a Single protein structure of sequence from Scapharca inaequivalvis. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of oxygenated Scapharca dimeric hemoglobin at 1.7-A resolution., Condon PJ, Royer WE Jr, J Biol Chem. 1994 Oct 14;269(41):25259-67. PMID:7929217
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