6KSC
Structural basis for domain rotation during adenylation of active site K123 and fragment library screening against NAD+ -dependent DNA ligase from Mycobacterium tuberculosis
Summary for 6KSC
Entry DOI | 10.2210/pdb6ksc/pdb |
Descriptor | DNA ligase A, ADENOSINE MONOPHOSPHATE, SULFATE ION, ... (4 entities in total) |
Functional Keywords | ligase |
Biological source | Mycobacterium tuberculosis H37Rv |
Total number of polymer chains | 1 |
Total formula weight | 37471.52 |
Authors | Ramachandran, R.,Shukla, A.,Afsar, M. (deposition date: 2019-08-23, release date: 2020-08-26, Last modification date: 2023-11-22) |
Primary citation | Afsar, M.,Shukla, A.,Kumar, N.,Ramachandran, R. Salt bridges at the subdomain interfaces of the adenylation domain and active-site residues of Mycobacterium tuberculosis NAD + -dependent DNA ligase A (MtbLigA) are important for the initial steps of nick-sealing activity. Acta Crystallogr D Struct Biol, 77:776-789, 2021 Cited by PubMed: 34076591DOI: 10.1107/S2059798321003107 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
Download full validation report