1THB

REFINEMENT OF A PARTIALLY OXYGENATED T STATE HAEMOGLOBIN AT 1.5 ANGSTROMS RESOLUTION

Summary for 1THB

• Entry DOI: 10.2210/pdb1thb/pdb
• Descriptor: HEMOGLOBIN A (OXY) (ALPHA CHAIN), HEMOGLOBIN A (DEOXY) (BETA CHAIN), PROTOPORPHYRIN IX CONTAINING FE, ... (6 entities in total)
• Functional Keywords: oxygen transport
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 4
• Total formula weight: 65271.08

Authors

Waller, D.A.,Liddington, R.C. (deposition date: 1990-01-23, release date: 1991-01-15, Last modification date: 2024-05-22)

Primary citation

Waller, D.A.,Liddington, R.C.
Refinement of a partially oxygenated T state human haemoglobin at 1.5 A resolution.
Acta Crystallogr.,Sect.B, 46:409-418, 1990

PubMed Abstract: The degree of ligation of T state human haemoglobin crystals is reduced by inositol hexaphosphate (IHP). The structure of a partially ligated haemoglobin has been refined using fast Fourier restrained-least-squares techniques. Manual interventions were required to escape from local minima and introduce a large number of solvent molecules. Individual isotropic temperature factors were refined for all atoms and the final average atomic temperature factor is 32.3 A2. The final R factor is 19.6% for all data between 10 and 1.5 A. The final model consists of 4560 protein atoms and 313 solvent molecules. The occupancies of the ligand atoms and the anisotropic behaviour of the iron atoms have been refined, demonstrating that the alpha haem groups are only partially ligated and that there is no ligation of the beta haems. Density for the IHP indicates that it is not well ordered even though changes in the ligation and structure of the haemoglobin indicate its presence.

PubMed: 2383372
DOI: 10.1107/S0108768190000313

Experimental method

X-RAY DIFFRACTION (1.5 Å)