3D7O
Human hemoglobin, nitrogen dioxide anion modified
Summary for 3D7O
| Entry DOI | 10.2210/pdb3d7o/pdb |
| Descriptor | Hemoglobin subunit alpha, Hemoglobin subunit beta, NITRITE ION, ... (6 entities in total) |
| Functional Keywords | human hemoglobin, acetylation, disease mutation, glycation, glycoprotein, heme, iron, metal-binding, oxygen transport, polymorphism, transport, hypotensive agent, pyruvate, s-nitrosylation, vasoactive |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 32457.67 |
| Authors | Yi, J.,Safo, M.K.,Richter-Addo, G.B. (deposition date: 2008-05-21, release date: 2009-05-05, Last modification date: 2023-08-30) |
| Primary citation | Yi, J.,Safo, M.K.,Richter-Addo, G.B. The nitrite anion binds to human hemoglobin via the uncommon O-nitrito mode. Biochemistry, 47:8247-8249, 2008 Cited by PubMed Abstract: The nitrite anion is known to oxidize and degrade hemoglobin (Hb). Recent literature reports suggest a nitrite reductase activity for Hb, converting nitrite into nitric oxide. Surprisingly, no structural information about Hb-nitrite interactions has been reported. We have determined the crystal structure of the ferric Hb-nitrite complex at 1.80 A resolution. The nitrite ligand adopts the uncommon O-nitrito binding mode. In addition, the nitrito conformations in the alpha and beta subunits are different, reflecting subtle effects of the distal His in orienting the nitrite ligand in the O-nitrito binding mode. PubMed: 18630930DOI: 10.1021/bi801015c PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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