About: Variations of the RMSD of α-helix3 (residues 96–126) along 1 μs MD trajectories in loop-in and helical conformations of several complexes, complexes with compounds 8, 14, 16, 20, and 1,6, with WT in blue and L107A in green.



Protein conformational flexibility modulates kinetics and thermodynamics of drug binding 6

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Scientist
M. Amaral D. B. Kokh, J. Bomke, A. Wegener,H. P. Buchstaller, H. M. Eggenweiler,P. Matias, C. Sirrenberg,R. C. Wade, and M. Frech
Protein
N-HSP90
Ligand
compounds 8, 14, 16, 20, and 1,6, respectively
Simulation Duration
InChIKey
HOPLWCOVETYSLA-VHWOAPHOSA-N
SMILES
CC[C@H](C)[C@H]1C(=O)N(CC(=O)N(CC(=O)N([C@H](C(=O)N(CC(=O)N[C@H](C(=O)N[C@H](C(=O)N(C(C(=O)N[C@H](C(=O)N([C@@H](CC(=O)N([C@H](C(=O)N1)CC(C)C)C)C)C)CC(C)C)(C)C)C)CC#C)CC2=CC(=CC=C2)I)C)CC3=CC=C(C=C3)C(F)(F)F)C)C)C
Molecular Formula
C63H91F3IN11O11
Protein Details
Hsp90 is a highly abundant and ubiquitous molecular chaperone which plays an essential role in many cellular processes including cell cycle control, cell survival, hormone and other signalling pathways. It is important for the cell's response to stress and is a key player in maintaining cellular homeostasis
Ligand Details
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