1NDH
CRYSTAL STRUCTURE OF NADH-CYTOCHROME B5 REDUCTASE FROM PIG LIVER AT 2.4 ANGSTROMS RESOLUTION
1NDH の概要
エントリーDOI | 10.2210/pdb1ndh/pdb |
分子名称 | CYTOCHROME B5 REDUCTASE, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total) |
機能のキーワード | electron transport (flavo protein) |
由来する生物種 | Sus scrofa (pig) |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 31659.22 |
構造登録者 | |
主引用文献 | Nishida, H.,Inaka, K.,Yamanaka, M.,Kaida, S.,Kobayashi, K.,Miki, K. Crystal structure of NADH-cytochrome b5 reductase from pig liver at 2.4 A resolution. Biochemistry, 34:2763-2767, 1995 Cited by PubMed Abstract: The three-dimensional structure of NADH-cytochrome b5 reductase from pig liver microsomes has been determined at 2.4 A resolution by X-ray crystallography. The molecular structure reveals two domains, the FAD binding domain and the NADH domain. A large cleft lies between these two domains and contains the binding site for the FAD prosthetic group. The backbone structure of the FAD binding domain has a great similarity to that of ferredoxin-NADP+ reductase [Karplus, P. A., Daniels, M. J., & Herriott, J. R. (1991) Science 251, 60-65], in spite of the relatively low sequence homology (about 15%) between the two enzymes. On the other hand, the structure of the NADH domain has several structural differences from that of the NADP+ domain of ferredoxin-NADP+ reductase. The size of the cleft between the two domains is larger in NADH-cytochrome b5 reductase than in ferredoxin-NADP+ reductase, which may be responsible for the observed difference in the nucleotide accessibility in the two enzymes. PubMed: 7893687DOI: 10.1021/bi00009a004 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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