Structure of crystalline alpha-chymotrypsin. 3. Crystallographic studies of substrates and inhibitors bound to the active site of alpha-chymotrypsin.
D001120:Arginine; D001224:Aspartic Acid; D001665:Binding Sites; D002918:Chymotrypsin / Q000037:antagonists & inhibitors*; D006639:Histidine; D007211:Indoles; D008239:Lysine; D008967:Molecular Biology; D010455:Peptides; D011485:Protein Binding; D012694:Serine; D014050:Toluene; D014357:Trypsin; D014364:Tryptophan; D014961:X-Ray Diffraction
D007211:Indoles; D010455:Peptides; D001224:Aspartic Acid; D014050:Toluene; D012694:Serine; D006639:Histidine; D014364:Tryptophan; D001120:Arginine; D002918:Chymotrypsin; D014357:Trypsin; D008239:Lysine