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EC Number Crystallization (Commentary)
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.109complexed with benzamidine or bovine panreatic trypsin inhibitor, hanging drop vapor diffusion method
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.109in complex with inhibitor D-hTyr-Ala-4-amidinobenzylamide
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.109molecular docking of inhibitor. The P1 and P2 binding sites are occupied by the conserved Arg and then the variable second side chain, respectively. The 9-fluorenylmethyloxycarbonyl group forms pi-pi interactions with the conserved Trp in the P4 pocket
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.109mutant N164Q/R614A/S805A, to 2.5 A resolution. The structure of zymogen matriptase reveals a classical chymotrypsin-like zymogen fold
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.109purified recombinant refolded His-tagged matriptase catalytic domain in complex with benzamidine, 2-Nas-Phe(3-Am)-4-(2-guanidinoethyl)piperidide, and 4-([1-[(2S)-3-(3-carbamimidoylphenyl)-2-([[2,4,6-tris(1-methylethyl)phenyl]sulfonyl]amino)propanoyl]piperidin-4-yl]carbonyl)piperidine-1-carboximidamide, hanging drop vapor diffusion method, 18°C, 5 mg/mL matriptase, from 10 mM benzamidine, 0.1 M Tris-HCl, pH 8.5, 20% PEG 8000, and 200 mM MgCl2, X-ray diffraction structure determination and analysis at 2.1-2.2 A resolution
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