6FQF
THE X-RAY STRUCTURE OF FERRIC-BETA4 HUMAN HEMOGLOBIN
Summary for 6FQF
| Entry DOI | 10.2210/pdb6fqf/pdb |
| Descriptor | Hemoglobin subunit beta, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
| Functional Keywords | human hemoglobin, oxygen transport |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 4 |
| Total formula weight | 66026.74 |
| Authors | Mazzarella, L.,Merlino, A.,Balasco, N.,Balsamo, A.,Vergara, A. (deposition date: 2018-02-14, release date: 2018-06-13, Last modification date: 2024-10-16) |
| Primary citation | Mazzarella, L.,Merlino, A.,Balasco, N.,Balsamo, A.,Vergara, A. Crystal structure of the ferric homotetrameric beta4human hemoglobin. Biophys. Chem., 240:9-14, 2018 Cited by PubMed Abstract: Spectroscopic studies carried out in the early seventies have shown that the β-homotetramer of human hemoglobin (β-HbA) in the ferric state is a mixture of aquomet and bis-histidyl forms. Here we present the first crystal structure, solved at 2.10 Å resolution, of the oxidized form of β-HbA. The overall quaternary structure of the protein in the ferric state is virtually indistinguishable from that of the ferrous deoxygenated and carbomonoxy forms. The structure reveals that the four hemes are exclusively in an aquomet coordination, without any trace of bis-histidyl coordination. The oxidation of β-HbA is associated with the formation of a disulfide bridge between residues Cys112(G14) of β/β and β/β chains. The coordination state of β-HbA has been compared to that known for other organisms that exhibit bis-histidyl heme coordination in the β state. This occurrence has been discussed in terms of different organism physiology. PubMed: 29857171DOI: 10.1016/j.bpc.2018.05.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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