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CCDC Gold Suite 5.3

cadcamaec@protonmail.com2024-01-29CAD.CAID94
TheCambridgeCrystallographicDataCentre(CCDC),aleadingproviderofstructuraldatabasesandso

The Cambridge Crystallographic Data Centre (CCDC), a leading provider of structural databases and software for pharmaceutical discovery, materials development, research and education, announce the release of GOLD Suite version 5.3 which contains new features, bug fixes and modifications.

GOLD has proven success in virtual screening, lead optimisation, and identifying the correct binding mode of active molecules.
Comprehensively validated and widely used, GOLD enables you to make confident binding mode predictions, and achieve high database enrichments. GOLD reliably identifies the correct binding mode for a large range of test set cases, and has been shown to perform favourably against other docking tools in numerous independent studies.

GOLD is highly configurable allowing you to take full advantage of your knowledge of a protein-ligand system in order to maximise docking performance. GOLD enables complete user control over speed versus accuracy settings, from efficient virtual screening of large compound libraries, to highly accurate exhaustive sampling for lead optimisation. With a wide range of available scoring functions and customisable docking protocols, GOLD provides consistently high performance across a diverse range of receptor types.

GOLD accounts for receptor flexibility through side-chain flexibility and most importantly ensemble docking. Using a novel methodology which avoids computationally expensive sequential docking of ligands into multiple protein structures, ensemble docking with GOLD solves the challenge of model selection.

A wide range of constraints can be employed to ensure, for example, that key H-bond interactions are fulfilled, or to bias docking results towards a known binding motif. Unfavourable ligand conformations can be eliminated by utilising customisable torsion angle distributions and an extensive library of ring conformations extracted from the Cambridge Structural Database.



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