3FV4

Thermolysin inhibition

Summary for 3FV4

Entry DOI	10.2210/pdb3fv4/pdb
Related	3ELF 4TMN 5TMN
Related PRD ID	PRD_000653
Descriptor	Thermolysin, CALCIUM ION, ZINC ION, ... (7 entities in total)
Functional Keywords	protease phosphonamidate inhibitor, hydrolase, metal-binding, metalloprotease, protease, secreted, zymogen
Biological source	Bacillus thermoproteolyticus
Total number of polymer chains	1
Total formula weight	35432.01
Authors	Englert, L.,Biela, A.,Heine, A.,Klebe, G. (deposition date: 2009-01-15, release date: 2010-02-09, Last modification date: 2023-09-06)
Primary citation	Englert, L.,Biela, A.,Zayed, M.,Heine, A.,Hangauer, D.,Klebe, G. Displacement of disordered water molecules from hydrophobic pocket creates enthalpic signature: binding of phosphonamidate to the S1'-pocket of thermolysin. Biochim.Biophys.Acta, 1800:1192-1202, 2010 Cited by PubMed Abstract: Prerequisite for the design of tight binding protein inhibitors and prediction of their properties is an in-depth understanding of the structural and thermodynamic details of the binding process. A series of closely related phosphonamidates was studied to elucidate the forces underlying their binding affinity to thermolysin. The investigated inhibitors are identical except for the parts penetrating into the hydrophobic S₁'-pocket. PubMed: 20600625 DOI: 10.1016/j.bbagen.2010.06.009 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.56 Å)

Structure validation