1hbs

Revision as of 13:58, 8 November 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1hbs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hbs, resolution 3.0Å" /> '''REFINED CRYSTAL STRU...)
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REFINED CRYSTAL STRUCTURE OF DEOXYHEMOGLOBIN S. I. RESTRAINED LEAST-SQUARES REFINEMENT AT 3.0-ANGSTROMS RESOLUTION

File:1hbs.gif


1hbs, resolution 3.0Å

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OverviewOverview

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 StructureAbout this Structure

1HBS is a Protein complex structure of sequences from Homo sapiens with HEM as ligand. Full crystallographic information is available from OCA.

ReferenceReference

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

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