Literature summary for 3.4.21.2 extracted from

Batra, J.; Szabo, A.; Caulfield, T.R.; Soares, A.S.; Sahin-Toth, M.; Radisky, E.S.
Long-range electrostatic complementarity governs substrate recognition by human chymotrypsin C, a key regulator of digestive enzyme activation (2013), J. Biol. Chem., 288, 9848-9859.

Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with small protease inhibitor eglin C, to 1.9 A resolution. The inhibitor binds in a substrate-like manner filling the S6-S5' subsites of the substrate binding cleft. Significant binding affinity derives from burial of preferred hydrophobic residues at the P1, P4, and P2' positions of chymotrypsin C, although acidic P2' residues can also be accommodated by formation of an interfacial salt bridge. There is a ring of intense positive electrostatic surface potential surrounding the primarily hydrophobic substrate binding site. Long-range electrostatic attraction toward substrates of concentrated negative charge governs substrate discrimination	Homo sapiens

Crystallization (Comment)

Organism

in complex with small protease inhibitor eglin C, to 1.9 A resolution. The inhibitor binds in a substrate-like manner filling the S6-S5' subsites of the substrate binding cleft. Significant binding affinity derives from burial of preferred hydrophobic residues at the P1, P4, and P2' positions of chymotrypsin C, although acidic P2' residues can also be accommodated by formation of an interfacial salt bridge. There is a ring of intense positive electrostatic surface potential surrounding the primarily hydrophobic substrate binding site. Long-range electrostatic attraction toward substrates of concentrated negative charge governs substrate discrimination

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q99895	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

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Release 2023.1 (January 2023)