3LKA

Catalytic domain of human MMP-12 complexed with hydroxamic acid and paramethoxy-sulfonyl amide

Summary for 3LKA

Entry DOI	10.2210/pdb3lka/pdb
Descriptor	Macrophage metalloelastase, ZINC ION, CALCIUM ION, ... (6 entities in total)
Functional Keywords	matrix metalloproteinase, mmp12, elastase, complex (elastase-inhibitor), metallo elastase, extracellular matrix, glycoprotein, hydrolase, metal-binding, metalloprotease
Biological source	Homo sapiens (human)
Cellular location	Secreted, extracellular space, extracellular matrix : P39900
Total number of polymer chains	1
Total formula weight	17997.81
Authors	Calderone, V. (deposition date: 2010-01-27, release date: 2010-05-12, Last modification date: 2023-09-06)
Primary citation	Borsi, V.,Calderone, V.,Fragai, M.,Luchinat, C.,Sarti, N. Entropic contribution to the linking coefficient in fragment based drug design: a case study. J.Med.Chem., 53:4285-4289, 2010 Cited by PubMed Abstract: For several drug leads obtained by tethering weak binding ligands, the dissociation constant is smaller than the product of those of the individual fragments by a factor named the linking coefficient, E. This favorable contribution is attributed to the entropic gain that is realized when two weak binding ligands are tethered. Here we show a case study where the linking coefficient is strikingly small (E = 2.1 x 10(-3) M(-1)) and its totally entropic nature is demonstrated. PubMed: 20415416 DOI: 10.1021/jm901723z PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.8 Å)

Structure validation