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Figure 2 | BMC Microbiology

Figure 2

From: The highly conserved serine threonine kinase StkP of Streptococcus pneumoniae contributes to penicillin susceptibility independently from genes encoding penicillin-binding proteins

Figure 2

Predicted structure of the kinase catalytic domain of StkP. (A) Image of backbone with oxygens of the StkP kinase domain (4–274). In white, predicted catalytic zones: ATP-binding site (18–42) and kinase motif (132–144). In green: Asp136 – phosphorylation site and Lys42 – ATP binding site. The amino acid substitutions, relative to the R6 sequence, are in red: Arg45Lys, Ala113Val, Asn227Lys and Ser237Pro. (B) Image of computed molecular surface of StkP kinase domain (4–274). The colours are otherwise as in Fig. 2A.

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BMC Microbiology

ISSN: 1471-2180

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