5B3P
Nqo5 of the trypsin-resistant fragment (1-134) in P212121 form
Summary for 5B3P
| Entry DOI | 10.2210/pdb5b3p/pdb |
| Related | 5B3Q |
| Descriptor | NADH-quinone oxidoreductase subunit 5, CALCIUM ION (3 entities in total) |
| Functional Keywords | nadh-ubiquinone oxidoreductase, complex i, oxidoreductase |
| Biological source | Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) |
| Total number of polymer chains | 1 |
| Total formula weight | 15767.00 |
| Authors | Hanazono, Y.,Takeda, K.,Miki, K. (deposition date: 2016-03-09, release date: 2016-07-27, Last modification date: 2024-03-20) |
| Primary citation | Hanazono, Y.,Takeda, K.,Miki, K. Characterization of the Nqo5 subunit of bacterial complex I in the isolated state Febs Open Bio, 6:687-695, 2016 Cited by PubMed Abstract: The subunits that comprise bacterial complex I (NADH:ubiquinone oxidoreductase) are also found in more complicated mitochondrial enzymes in eukaryotic organisms. Although the Nqo5 subunit is one of these conserved components and important for the formation of complex, it has been little studied. Here, we report structure analyses of isolated Nqo5 from Thermus thermophilus. Biochemical studies indicated that the C-terminal region following the 30-Kd subunit motif is disordered in the isolated state, while the remaining portion is already folded. Crystallographic studies of a trypsin-resistant fragment revealed detailed structural differences in the folded domain between the isolated and complexed states. PubMed: 27398308DOI: 10.1002/2211-5463.12070 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.652 Å) |
Structure validation
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