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2EIX

The Structure of Physarum polycephalum cytochrome b5 reductase

Summary for 2EIX
Entry DOI10.2210/pdb2eix/pdb
Related1UMK
DescriptorNADH-cytochrome b5 reductase, IODIDE ION, SODIUM ION, ... (6 entities in total)
Functional Keywordsflavoprotein, fad-binding domain, nadh-binding, oxidoreductase
Biological sourcePhysarum polycephalum
Total number of polymer chains2
Total formula weight57875.17
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 citationKim, 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: 17401193
DOI: 10.1107/S1744309107010731
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.56 Å)
Structure validation

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