Literature summary for 3.4.21.6 extracted from

Abel, R.; Young, T.; Farid, R.; Berne, B.J.; Friesner, R.A.
Role of the active-site solvent in the thermodynamics of factor Xa ligand binding (2008), J. Am. Chem. Soc., 130, 2817-2831.

Crystallization (Commentary)

Crystallization (Comment)	Organism
method for quantifying the contributions to the free energy of binding due to the ligand evacuating energetically unfavorable and entropically structured solvent for the set of congeneric pairs. The expulsion of active-site water strongly impacts protein-ligand binding affinities in two ways. Hydrophobic ligand groups that displace water from energetically unfavorable hydrophobically enclosed environments contribute enthalpically since the water molecules will make more favorable interactions in the bulk fluid. Ligand groups that displace entropically structured solvent contribute even when the solvent interacts favorably with the protein since well-designed ligands will recapture the protein-water interaction energy	Homo sapiens

Crystallization (Comment)

Organism

method for quantifying the contributions to the free energy of binding due to the ligand evacuating energetically unfavorable and entropically structured solvent for the set of congeneric pairs. The expulsion of active-site water strongly impacts protein-ligand binding affinities in two ways. Hydrophobic ligand groups that displace water from energetically unfavorable hydrophobically enclosed environments contribute enthalpically since the water molecules will make more favorable interactions in the bulk fluid. Ligand groups that displace entropically structured solvent contribute even when the solvent interacts favorably with the protein since well-designed ligands will recapture the protein-water interaction energy

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

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Release 2023.1 (January 2023)