5CKY
Crystal Structure of the MTERF1 R162A substitution bound to the termination sequence.
Summary for 5CKY
Entry DOI | 10.2210/pdb5cky/pdb |
Related | 5CO0 |
Descriptor | Transcription termination factor 1, mitochondrial, 5'-D(*AP*TP*TP*AP*CP*CP*GP*GP*GP*CP*TP*CP*TP*GP*CP*CP*AP*TP*CP*TP*TP*A)-3', 5' -D (*TP*AP*AP*GP*AP*TP*GP*GP*CP*AP*GP*AP*GP*CP*CP*CP*GP*GP*TP*AP*AP*T)-3', ... (4 entities in total) |
Functional Keywords | protein-dna, transcription factor, mitochondria, termination, transcription-dna complex, transcription/dna |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 3 |
Total formula weight | 50628.81 |
Authors | Byrnes, J.,Hauser, K.,Norona, L.,Mejia, E.,Simmerling, C.,Garcia-Diaz, M. (deposition date: 2015-07-15, release date: 2015-11-25, Last modification date: 2023-09-27) |
Primary citation | Byrnes, J.,Hauser, K.,Norona, L.,Mejia, E.,Simmerling, C.,Garcia-Diaz, M. Base Flipping by MTERF1 Can Accommodate Multiple Conformations and Occurs in a Stepwise Fashion. J.Mol.Biol., 428:2542-2556, 2016 Cited by PubMed: 26523681DOI: 10.1016/j.jmb.2015.10.021 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.62 Å) |
Structure validation
Download full validation report