Ensembler: Enabling High-Throughput Molecular Simulations at the Superfamily Scale
Fig 8
Two structures of Src, indicating certain residues involved in activation.
In the inactive state, E310 forms a salt bridge with R409. During activation, the αC-helix (green) moves and rotates, orienting E310 towards the ATP-binding site and allowing it to instead form a salt bridge with K295. This positions K295 in the appropriate position for catalysis. Note that ANP (phosphoaminophosphonic acid-adenylate ester; an analog of ATP) is only physically present in the 2SRC structure. To aid visualization of the active site in 1Y57, it has been included in the rendering by structurally aligning the surrounding homologous protein residues.