3EHV

X-ray structure of human ubiquitin Zn(II) adduct

Summary for 3EHV

• Entry DOI: 10.2210/pdb3ehv/pdb
• Related: 1UBQ 3EEC 3EFU
• Descriptor: Ubiquitin, ZINC ION (3 entities in total)
• Functional Keywords: human ubiquitin, adduct, ligase
• Biological source: Homo sapiens
• Total number of polymer chains: 3
• Total formula weight: 25795.90

Authors

Falini, G.,Fermani, S.,Tosi, G. (deposition date: 2008-09-15, release date: 2009-03-17, Last modification date: 2023-11-01)

Primary citation

Falini, G.,Fermani, S.,Tosi, G.,Arnesano, F.,Natile, G.
Structural probing of Zn(II), Cd(II) and Hg(II) binding to human ubiquitin.
Chem.Commun.(Camb.), 45:5960-5962, 2008

PubMed Abstract: A structural investigation performed on adducts of human ubiquitin with group-12 metal ions reveals common preferential anchoring sites, the most populated one being His68; at higher metal ion concentration a second and a third site, close to the N-terminus of the protein, become populated and promote a polymorphic transition from orthorhombic to cubic form; Glu16 and Glu18, involved in the latter metal binding, undergo a remarkable displacement from their position in native ubiquitin; the aggregate stereochemistry appears to be driven by the clustering of deshielded backbone hydrogen-bond patches, and metal ions foster this process.

PubMed: 19030552
DOI: 10.1039/b813463d

Experimental method

X-RAY DIFFRACTION (1.81 Å)