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EC Number Crystallization (Commentary) Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.B5homology modeling of protease in complex with amprenavir. The amino acids at the active site of HIV-1, HTLV proteases and those likely to be at the active site of XMRV protease are comparatively conserved. Amprenavir interacts with residue Asp32 of the catalytic domain, and also contacts the residues Val39, Lys61, Tyr90, and Leu92. A water molecule would intermediate interactions between amprenavir and Ala57 734565
Display the word mapDisplay the reaction diagram Show all sequences 3.4.23.B5in complex with inhibitors amprenavir, pepstatin A and TL-3, to 1.75, 1.5 and 1.4 A resolution, respectively. TL-3 and amprenavir bind in a predictable manner, spanning the substrate-binding site of the enzyme, while two molecules of pepstatin A bind simultaneously, leaving the catalytic water molecule in place 717598
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