1c4p

BETA DOMAIN OF STREPTOKINASE

spinqualitylabelsall models 1c4p, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1c4p is a 4 chain structure with sequence from Streptococcus dysgalactiae subsp. equisimilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q53284_STREQ Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Crystal structure of streptokinase beta-domain.,Wang X, Tang J, Hunter B, Zhang XC FEBS Lett. 1999 Oct 1;459(1):85-9. PMID:10508922 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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