Structural highlights
3ehv is a 3 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | |
| Related: | 1ubq, 3eec, 3efu |
| Gene: | RPS27A, UBA80, UBCEP1, UBA52, UBCEP2, UBB, UBC (HUMAN) |
| Activity: | Ubiquitin--protein ligase, with EC number 6.3.2.19 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structural probing of Zn(ii), Cd(ii) and Hg(ii) binding to human ubiquitin.,Falini G, Fermani S, Tosi G, Arnesano F, Natile G Chem Commun (Camb). 2008 Dec 7;(45):5960-2. Epub 2008 Oct 9. PMID:19030552[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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). 2008 Dec 7;(45):5960-2. Epub 2008 Oct 9. PMID:19030552 doi:10.1039/b813463d
