2yec | pdb_00002yec

HSP90 inhibitors and drugs from fragment and virtual screening

spinqualitylabelsall models 2yec, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2yec is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4, XQ0 Related: 2cdd, 1yes, 1uy9, 1byq, 2bsm, 1osf, 2wi3, 1uy8, 2bug, 2wi4, 2uwd, 2xhx, 2wi7, 2bt0, 1yer, 2xdu, 1uyg, 2bz5, 2ccu, 2xds, 2xdx, 2xk2, 2ccs, 1uyf, 1yc3, 1uyi, 2xjj, 1uyd, 2byi, 2xdl, 2wi2, 1uy6, 2vci, 2wi1, 2vcj, 1yc4, 2xjx, 2c2l, 2fwz, 2xdk, 1uyh, 2xjg, 1uyk, 2cct, 2fwy, 1uyl, 1uye, 2wi6, 2xab, 1yc1, 1uyc, 2xhr, 2xht, 1uy7, 1yet, 2jjc, 2byh, 2wi5, 2yee, 2ye2, 2ye9, 2yeb, 2ye7, 2ye4, 2yej, 2ye5, 2yea, 2yeh, 2ye6, 2yed, 2yei, 2yeg, 2yef, 2ye8, 2ye3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [HS90A_HUMAN] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. See Also Heat Shock Protein structures

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