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5CKY

Crystal Structure of the MTERF1 R162A substitution bound to the termination sequence.

Summary for 5CKY
Entry DOI10.2210/pdb5cky/pdb
Related5CO0
DescriptorTranscription 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 Keywordsprotein-dna, transcription factor, mitochondria, termination, transcription-dna complex, transcription/dna
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains3
Total formula weight50628.81
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 citationByrnes, 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: 26523681
DOI: 10.1016/j.jmb.2015.10.021
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.62 Å)
Structure validation

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