Glyco3D

Glyco3D provides interlinked databases of three-dimensional structures of carbohydrates and carbohydrate-binding proteins to support structural glycobiology research.

Key Features:

• Extensive Database Coverage: Contains structures and related data for monosaccharides, disaccharides, oligosaccharides, polysaccharides, glycosyltransferases, lectins, monoclonal antibodies, and glycosaminoglycan-binding proteins.
• Annotated NMR Data: Includes annotated Nuclear Magnetic Resonance (NMR) data for bioactive oligosaccharides to inform three-dimensional configurations and interactions.
• Standardized Structural Encoding: Employs a common nomenclature system across databases for consistent structural encoding of carbohydrates.
• Specialized Databases: Comprises separate, focused databases for specific families of complex carbohydrates and carbohydrate-binding proteins.
• Advanced Search Engine: Provides a search engine capable of querying sequential carbohydrate information across all databases.
• Interconnected Databases: Interlinks entries to enable exploration of oligosaccharide conformational variability in vacuum, crystalline states, and when interacting with diverse proteins.

Scientific Applications:

• Three-dimensional structural analysis: Enables analysis of 3D structures of complex carbohydrates and carbohydrate-binding proteins.
• Conformational studies: Supports investigation of oligosaccharide conformational changes in vacuum, crystalline, and protein-bound environments.
• NMR interpretation: Facilitates interpretation of annotated NMR data for bioactive oligosaccharides.
• Comparative family analysis: Allows comparative studies across carbohydrate and carbohydrate-binding protein families using standardized encoding and specialized databases.

Methodology:

Databases are manually curated and developed using nonproprietary software; they use a common carbohydrate nomenclature, include annotated NMR data, interlink specialized databases, and provide a search engine for sequential carbohydrate queries to enable comparison of 3D conformations in vacuum, crystalline, and protein-bound contexts.