11RJ

D189A thrombin inhibited with D-Phe-Pro-Arg-Chloromethylketone

Summary for 11RJ

Entry DOI	10.2210/pdb11rj/pdb
Descriptor	Thrombin heavy chain, Thrombin light chain, D-phenylalanyl-N-[(2S,3S)-6-{[amino(iminio)methyl]amino}-1-chloro-2-hydroxyhexan-3-yl]-L-prolinamide, ... (5 entities in total)
Functional Keywords	serine protease, inhibitor, blood clotting
Biological source	Homo sapiens (human) More
Total number of polymer chains	2
Total formula weight	37499.18
Authors	Friet, T.,Mohammed, B.M.,Sukumar, N.,Di Cera, E. (deposition date: 2026-03-10, release date: 2026-10-07)
Primary citation	Friet, T.,Mikhail, G.,Mohammed, B.M.,Pelc, L.A.,Dei Rossi, A.,Korolev, S.,Di Cera, E. Structural analysis of the primary specificity of thrombin. J.Thromb.Haemost., 2026 Cited by PubMed Abstract: Thrombin has dual trypsin-like and chymotrypsin-like specificity: it prefers substrates carrying Arg at the site of cleavage (P1) in the activation peptide because of the presence of D189 in the primary specificity (S1) site but can also cleave substrates carrying Phe at P1. PubMed: 42767507 DOI: 10.1016/j.jtha.2026.09.021 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.5 Å)

Structure validation