6KDU

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 6KDU

Entry DOI	10.2210/pdb6kdu/pdb
Descriptor	DNA ligase A, ADENOSINE MONOPHOSPHATE, BETA-NICOTINAMIDE RIBOSE MONOPHOSPHATE, ... (5 entities in total)
Functional Keywords	ligase, dna binding protein
Biological source	Mycobacterium tuberculosis H37Rv
Total number of polymer chains	1
Total formula weight	37816.76
Authors	Ramachandran, R.,Shukla, A.,Afsar, M. (deposition date: 2019-07-02, release date: 2020-07-01, 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: 34076591 DOI: 10.1107/S2059798321003107 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.2 Å)

Structure validation