11RK

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

This is a non-PDB format compatible entry.

Summary for 11RK

• Entry DOI: 10.2210/pdb11rk/pdb
• Descriptor: Thrombin light chain, Thrombin heavy chain, SODIUM ION, ... (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: 37489.16

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

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

Experimental method

X-RAY DIFFRACTION (2.12 Å)