5G21

Leishmania major N-myristoyltransferase in complex with a quinoline inhibitor (compound 26).

Summary for 5G21

Entry DOI	10.2210/pdb5g21/pdb
Related	5G1Z 5G20 5G22
Descriptor	GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE, MAGNESIUM ION, TETRADECANOYL-COA, ... (5 entities in total)
Functional Keywords	transferase, myristoylation, malaria, inhibitor, drug design, quinoline
Biological source	LEISHMANIA MAJOR
Total number of polymer chains	1
Total formula weight	48989.90
Authors	Goncalves, V.,Brannigan, J.A.,Laporte, A.,Bell, A.S.,Roberts, S.M.,Wilkinson, A.J.,Leatherbarrow, R.J.,Tate, E.W. (deposition date: 2016-04-06, release date: 2017-02-15, Last modification date: 2017-06-28)
Primary citation	Goncalves, V.,Brannigan, J.A.,Laporte, A.,Bell, A.S.,Roberts, S.M.,Wilkinson, A.J.,Leatherbarrow, R.J.,Tate, E.W. Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase. Medchemcomm, 8:191-197, 2017 Cited by PubMed Abstract: The parasite is the most widely distributed cause of recurring malaria. -Myristoyltransferase (NMT), an enzyme that catalyses the covalent attachment of myristate to the N-terminal glycine of substrate proteins, has been described as a potential target for the treatment of this disease. Herein, we report the synthesis and the structure-guided optimization of a series of quinolines with balanced activity against both and -myristoyltransferase (NMT). PubMed: 28626547 DOI: 10.1039/c6md00531d PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.5 Å)

Structure validation