5GV7
Structure of NADH-cytochrome b5 reductase refined with the multipolar atomic model at 0.80 A
Summary for 5GV7
| Entry DOI | 10.2210/pdb5gv7/pdb |
| Related | 5GV8 |
| Descriptor | NADH-cytochrome b5 reductase 3, FLAVIN-ADENINE DINUCLEOTIDE, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | oxidoreductase, electron transfer, flavoprotein |
| Biological source | Sus scrofa (Pig) |
| Cellular location | Endoplasmic reticulum membrane ; Lipid-anchor ; Cytoplasmic side : P83686 |
| Total number of polymer chains | 1 |
| Total formula weight | 32027.60 |
| Authors | Takaba, K.,Takeda, K.,Miki, K. (deposition date: 2016-09-03, release date: 2017-04-05, Last modification date: 2023-11-08) |
| Primary citation | Takaba, K.,Takeda, K.,Kosugi, M.,Tamada, T.,Miki, K. Distribution of valence electrons of the flavin cofactor in NADH-cytochrome b5 reductase. Sci Rep, 7:43162-43162, 2017 Cited by PubMed Abstract: Flavin compounds such as flavin adenine dinucleotide (FAD), flavin mononucleotide and riboflavin make up the active centers in flavoproteins that facilitate various oxidoreductive processes. The fine structural features of the hydrogens and valence electrons of the flavin molecules in the protein environment are critical to the functions of the flavoproteins. However, information on these features cannot be obtained from conventional protein X-ray analyses at ordinary resolution. Here we report the charge density analysis of a flavoenzyme, NADH-cytochrome b reductase (b5R), at an ultra-high resolution of 0.78 Å. Valence electrons on the FAD cofactor as well as the peptide portion, which are clearly visualized even after the conventional refinement, are analyzed by the multipolar atomic model refinement. The topological analysis for the determined electron density reveals the valence electronic structure of the isoalloxazine ring of FAD and hydrogen-bonding interactions with the protein environment. The tetrahedral electronic distribution around the N5 atom of FAD in b5R is stabilized by hydrogen bonding with CH of Tyr65 and amide-H of Thr66. The hydrogen bonding network leads to His49 composing the cytochrome b-binding site via non-classical hydrogen bonds between N5 of FAD and CH of Tyr65 and O of Tyr65 and CH of His49. PubMed: 28225078DOI: 10.1038/srep43162 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (0.8 Å) |
Structure validation
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