Mobi 2.0

Mobi 2.0 annotates mobile regions and intrinsic disorder in protein structures to support analysis of protein dynamics.

Key Features:

• Robust Definitions of Mobility: Uses four indicators to define mobility: missing residues in PDB structures, elevated temperature factors (B-factors), inter-model variability among structure models, and mobility associated with binding to other proteins or nucleotides.
• Consensus Annotations: Aggregates data across multiple PDB structures mapped to a given UniProt protein sequence to produce consensus annotations of mobile regions.
• Standardization of Mobility Analysis: Applies uniform definitions and methodologies to enable consistent comparison of intrinsic disorder and mobility annotations across studies.
• Integration with MobiDB: Contributes structure-based mobility and disorder annotations to the MobiDB database.

Scientific Applications:

• Intrinsically Disordered Proteins (IDPs): Identifies and annotates mobile regions characteristic of proteins that lack a unique folded structure.
• Signaling and Molecular Recognition: Supports analysis of flexible regions involved in signaling pathways and molecular recognition events.
• Enzymatic Activity and Function: Annotates flexible segments relevant to enzymatic activity and functional modulation.
• Interaction Networks and Disease Mechanisms: Facilitates study of protein–protein and protein–nucleotide interactions and the implications of structural flexibility for disease mechanisms.

Methodology:

Performs comprehensive analysis of PDB data using indicators of mobility—missing residues, temperature factors (B-factors), inter-model variability, and binding-associated mobility—and aggregates structure-based annotations mapped to UniProt sequences to generate consensus annotations.