2EIX
The Structure of Physarum polycephalum cytochrome b5 reductase
Summary for 2EIX
Entry DOI | 10.2210/pdb2eix/pdb |
Related | 1UMK |
Descriptor | NADH-cytochrome b5 reductase, IODIDE ION, SODIUM ION, ... (6 entities in total) |
Functional Keywords | flavoprotein, fad-binding domain, nadh-binding, oxidoreductase |
Biological source | Physarum polycephalum |
Total number of polymer chains | 2 |
Total formula weight | 57875.17 |
Authors | Kim, S.W.,Suga, M.,Ogasahara, K.,Ikegami, T.,Minami, Y.,Yubisui, T.,Tsukihara, T. (deposition date: 2007-03-14, release date: 2007-04-17, Last modification date: 2023-10-25) |
Primary citation | Kim, S.,Suga, M.,Ogasahara, K.,Ikegami, T.,Minami, Y.,Yubisui, T.,Tsukihara, T. Structure of Physarum polycephalum cytochrome b5 reductase at 1.56 A resolution. Acta Crystallogr.,Sect.F, 63:274-279, 2007 Cited by PubMed Abstract: Physarum polycephalum cytochrome b(5) reductase catalyzes the reduction of cytochrome b(5) by NADH. The structure of P. polycephalum cytochrome b(5) reductase was determined at a resolution of 1.56 A. The molecular structure was compared with that of human cytochrome b(5) reductase, which had previously been determined at 1.75 A resolution [Bando et al. (2004), Acta Cryst. D60, 1929-1934]. The high-resolution structure revealed conformational differences between the two enzymes in the adenosine moiety of the FAD, the lid region and the linker region. The structural properties of both proteins were inspected in terms of hydrogen bonding, ion pairs, accessible surface area and cavity volume. The differences in these structural properties between the two proteins were consistent with estimates of their thermostabilities obtained from differential scanning calorimetry data. PubMed: 17401193DOI: 10.1107/S1744309107010731 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.56 Å) |
Structure validation
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