4N8T
Human hemoglobin nitric oxide adduct
Summary for 4N8T
| Entry DOI | 10.2210/pdb4n8t/pdb |
| Descriptor | Hemoglobin subunit alpha, Hemoglobin subunit beta, PROTOPORPHYRIN IX CONTAINING FE, ... (7 entities in total) |
| Functional Keywords | human hemoglobin, nitric oxide, oxygen transport |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 32655.96 |
| Authors | Yi, J.,Richter-Addo, G.B. (deposition date: 2013-10-18, release date: 2014-10-08, Last modification date: 2023-09-20) |
| Primary citation | Yi, J.,Soares, A.S.,Richter-Addo, G.B. Crystallographic characterization of the nitric oxide derivative of R-state human hemoglobin. Nitric Oxide, 39:46-50, 2014 Cited by PubMed Abstract: Nitric oxide (NO) is a signaling agent that is biosynthesized in vivo. NO binds to the heme center in human hemoglobin (Hb) to form the HbNO adduct. This reaction of NO with Hb has been studied for many decades. Of continued interest has been the effect that the bound NO ligand has on the geometrical parameters of the resulting heme-NO active site. Although the crystal structure of a T-state human HbNO complex has been published previously, that of the high affinity R-state HbNO derivative has not been reported to date. We have crystallized and solved the three-dimensional X-ray structure of R-state human HbNO to 1.90 Å resolution. The differences in the FeNO bond parameters and H-bonding patterns between the α and β subunits contribute to understanding of the observed enhanced stability of the α(FeNO) moieties relative to the β(FeNO) moieties in human R-state HbNO. PubMed: 24769418DOI: 10.1016/j.niox.2014.04.001 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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