1BML

COMPLEX OF THE CATALYTIC DOMAIN OF HUMAN PLASMIN AND STREPTOKINASE

Summary for 1BML

• Entry DOI: 10.2210/pdb1bml/pdb
• Descriptor: PLASMIN, STREPTOKINASE (2 entities in total)
• Functional Keywords: human plasmin, streptokinase, blood clotting
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted : P00747
• Total number of polymer chains: 4
• Total formula weight: 136956.70

Authors

Wang, X.,Zhang, X.C. (deposition date: 1999-05-25, release date: 1999-08-02, Last modification date: 2024-10-16)

Primary citation

Wang, X.,Lin, X.,Loy, J.A.,Tang, J.,Zhang, X.C.
Crystal structure of the catalytic domain of human plasmin complexed with streptokinase.
Science, 281:1662-1665, 1998

PubMed Abstract: Streptokinase is a plasminogen activator widely used in treating blood-clotting disorders. Complexes of streptokinase with human plasminogen can hydrolytically activate other plasminogen molecules to plasmin, which then dissolves blood clots. A similar binding activation mechanism also occurs in some key steps of blood coagulation. The crystal structure of streptokinase complexed with the catalytic unit of human plasmin was solved at 2.9 angstroms. The amino-terminal domain of streptokinase in the complex is hypothesized to enhance the substrate recognition. The carboxyl-terminal domain of streptokinase, which binds near the activation loop of plasminogen, is likely responsible for the contact activation of plasminogen in the complex.

PubMed: 9733510
DOI: 10.1126/science.281.5383.1662

Experimental method

X-RAY DIFFRACTION (2.9 Å)