1C4P

BETA DOMAIN OF STREPTOKINASE

Summary for 1C4P

• Entry DOI: 10.2210/pdb1c4p/pdb
• Related: 1BML
• Descriptor: PROTEIN (STREPTOKINASE) (2 entities in total)
• Functional Keywords: plasminogen activator, blood clotting
• Biological source: Streptococcus dysgalactiae subsp. equisimilis
• Total number of polymer chains: 4
• Total formula weight: 63322.62

Authors

Wang, X.,Zhang, X.C. (deposition date: 1999-09-15, release date: 1999-10-13, Last modification date: 2023-12-27)

Primary citation

Wang, X.,Tang, J.,Hunter, B.,Zhang, X.C.
Crystal structure of streptokinase beta-domain.
FEBS Lett., 459:85-89, 1999

PubMed Abstract: Streptokinase, a 47 kDa secreted protein of hemolytic strains of streptococci, is a human plasminogen activator and contains three structural domains linked by flexible loops. We describe here the crystal structure of the isolated streptokinase middle (SKbeta) domain determined at 2.4 A resolution. Among the functionally important structural features is a putative binding site for a kringle domain of plasminogen located at the tip of a fully exposed hairpin loop. The distribution of genetically conserved residues of SKbeta is strongly correlated with their functions. The extensive interface of the SKbeta dimer suggests that such dimers may also exist in solution for free SKbeta.

PubMed: 10508922
DOI: 10.1016/S0014-5793(99)01214-4

Experimental method

X-RAY DIFFRACTION (2.4 Å)