2OOA: UBA domain from Cbl-b ubiquitin ligase

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.

Method
X-ray diffraction
Resolution
1.56 Å
Organism
Homo sapiens
Chains
2
Atoms
796
Mol. weight
11.41 kDa
Released
6 Feb 2007

Explore 2OOA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chains A and B: 3 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix933-9419
α-helix946-95510
α-helix960-97011

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
E3 ubiquitin-protein ligase CBL-BA, Bprotein52Homo sapiensQ13191 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>2OOA_1 E3 ubiquitin-protein ligase CBL-B (chains A, B)
GSGPEAALENVDAKIAKLMGEGYAFEEVKRALEIAQNNVEVARSILREFAFP

Primary citation

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:

Browse structure collections

About this viewer

MolViewer shows 2OOA directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.