1HBS

REFINED CRYSTAL STRUCTURE OF DEOXYHEMOGLOBIN S. I. RESTRAINED LEAST-SQUARES REFINEMENT AT 3.0-ANGSTROMS RESOLUTION

Summary for 1HBS

• Entry DOI: 10.2210/pdb1hbs/pdb
• Descriptor: HEMOGLOBIN S (DEOXY) (ALPHA CHAIN), HEMOGLOBIN S (DEOXY) (BETA CHAIN), PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: oxygen transport
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 8
• Total formula weight: 128974.17

Authors

Padlan, E.A.,Love, W.E. (deposition date: 1982-06-02, release date: 1982-07-29, Last modification date: 2024-02-07)

Primary citation

Padlan, E.A.,Love, W.E.
Refined crystal structure of deoxyhemoglobin S. I. Restrained least-squares refinement at 3.0-A resolution.
J.Biol.Chem., 260:8272-8279, 1985

PubMed Abstract: The crystal structure of deoxyhemoglobin S has been refined at 3.0-A resolution using the Hendrickson-Konnert restrained least-squares method. Comparison with the structure of deoxyhemoglobin A reveals a hingelike movement of the beta-chain A helices, which are involved in molecular contacts, toward the EF corners of their respective subunits. This movement brings the amino termini of the beta-chains closer to the molecular dyad. The A helices remain alpha-helical throughout their entire lengths. No other major structural difference is found between deoxyhemoglobin A and deoxyhemoglobin S.

PubMed: 4008491

Experimental method

X-RAY DIFFRACTION (3 Å)