Mouse UBAh-Ubiquitin Complex NMR Structure Data

NMR structure data for the mouse UBAh–ubiquitin complex, supporting figures in a study by Nobukazu Nameki. The dataset includes structural details and binding affinity measurements, such as a dissociation constant of approximately 50 µM. It was last updated on June 3, 2026.

Use Cases

• Analyze protein-protein interaction modes based on NMR-derived structural coordinates
• Validate computational models of ubiquitin binding based on the reported hydrophobic patch interactions
• Compare binding affinities of protein domains based on the reported dissociation constant
• Study ribosome recruitment mechanisms based on the structural insights into the UBAh domain

Strengths

• Includes a specific dissociation constant measurement of approximately 50 µM
• Provides structural insights into a unique protein domain (UBAh) with a three-helix bundle architecture
• Data is associated with specific published figures (Fig 6A, S4D Fig, S11 Fig)

Limitations

• Column-level documentation is absent; field semantics must be inferred after download
• Row count is unknown, which may limit suitability assessment
• The dataset is very small (15.0 KB), indicating limited scope

Provenance

Source

figshare

Freshness

Last updated 2026-06-03 17:42:38; freshness should be verified