1hbs
From Proteopedia
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| , resolution 3.0Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
REFINED CRYSTAL STRUCTURE OF DEOXYHEMOGLOBIN S. I. RESTRAINED LEAST-SQUARES REFINEMENT AT 3.0-ANGSTROMS RESOLUTION
Overview
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.
About this Structure
1HBS is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Refined crystal structure of deoxyhemoglobin S. I. Restrained least-squares refinement at 3.0-A resolution., Padlan EA, Love WE, J Biol Chem. 1985 Jul 15;260(14):8272-9. PMID:4008491
Page seeded by OCA on Sun Mar 30 21:01:48 2008
