1ndh
From Proteopedia
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CRYSTAL STRUCTURE OF NADH-CYTOCHROME B5 REDUCTASE FROM PIG LIVER AT 2.4 ANGSTROMS RESOLUTION
Overview
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.
About this Structure
1NDH is a Single protein structure of sequence from Sus scrofa with FAD as ligand. Active as Cytochrome-b5 reductase, with EC number 1.6.2.2 Full crystallographic information is available from OCA.
Reference
Crystal structure of NADH-cytochrome b5 reductase from pig liver at 2.4 A resolution., Nishida H, Inaka K, Yamanaka M, Kaida S, Kobayashi K, Miki K, Biochemistry. 1995 Mar 7;34(9):2763-7. PMID:7893687
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