crystal structure of the UBA domain from Cbl-b ubiquitin ligase. Determined by X-ray diffraction at 1.56 Å resolution. Released 6 Feb 2007.
Explore 2OOA in 3D Show helices and sheets RCSB PDB PDBe
2OOA contains 6 α-helices and 0 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 933-941 | 9 | |
| α-helix | 946-955 | 10 | |
| α-helix | 960-970 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| E3 ubiquitin-protein ligase CBL-B | A, B | protein | 52 | Homo sapiens | Q13191 (AlphaFold model) |
>2OOA_1 E3 ubiquitin-protein ligase CBL-B (chains A, B) GSGPEAALENVDAKIAKLMGEGYAFEEVKRALEIAQNNVEVARSILREFAFP
Structural basis for ubiquitin-mediated dimerization and activation of the ubiquitin protein ligase Cbl-b. Peschard, P., Kozlov, G., Lin, T. et al. Mol Cell (2007) 27:474-485. DOI 10.1016/j.molcel.2007.06.023 · PubMed
Other PDB entries of the same protein (UniProt Q13191 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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