1UMK
The Structure of Human Erythrocyte NADH-cytochrome b5 Reductase
Summary for 1UMK
| Entry DOI | 10.2210/pdb1umk/pdb |
| Descriptor | NADH-cytochrome b5 reductase, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total) |
| Functional Keywords | flavoprotein, beta barrel, fad-binding domain, nadh-binding domain, oxidoreductase |
| Biological source | Homo sapiens (human) |
| Cellular location | Isoform 1: Endoplasmic reticulum membrane; Lipid-anchor; Cytoplasmic side. Isoform 2: Cytoplasm: P00387 |
| Total number of polymer chains | 1 |
| Total formula weight | 32084.69 |
| Authors | Bando, S.,Takano, T.,Yubisui, T.,Shirabe, K.,Takeshita, M.,Horii, C.,Nakagawa, A. (deposition date: 2003-10-03, release date: 2004-11-02, Last modification date: 2023-12-27) |
| Primary citation | Bando, S.,Takano, T.,Yubisui, T.,Shirabe, K.,Takeshita, M.,Nakagawa, A. Structure of human erythrocyte NADH-cytochrome b5 reductase. Acta Crystallogr.,Sect.D, 60:1929-1934, 2004 Cited by PubMed Abstract: Erythrocyte NADH-cytochrome b(5) reductase reduces methaemoglobin to functional haemoglobin. In order to examine the function of the enzyme, the structure of NADH-cytochrome b(5) reductase from human erythrocytes has been determined and refined by X-ray crystallography. At 1.75 A resolution, the root-mean-square deviations (r.m.s.d.) from standard bond lengths and angles are 0.006 A and 1.03 degrees , respectively. The molecular structure was compared with those of rat NADH-cytochrome b(5) reductase and corn nitrate reductase. The human reductase resembles the rat reductase in overall structure as well as in many side chains. Nevertheless, there is a large main-chain shift from the human reductase to the rat reductase or the corn reductase caused by a single-residue replacement from proline to threonine. A model of the complex between cytochrome b(5) and the human reductase has been built and compared with that of the haem-containing domain of the nitrate reductase molecule. The interaction between cytochrome b(5) and the human reductase differs from that of the nitrate reductase because of differences in the amino-acid sequences. The structures around 15 mutation sites of the human reductase have been examined for the influence of residue substitutions using the program ROTAMER. Five mutations in the FAD-binding domain seem to be related to cytochrome b(5). PubMed: 15502298DOI: 10.1107/S0907444904020645 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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