2OOB: UBA domain from Cbl-b ubiquitin ligase

crystal structure of the UBA domain from Cbl-b ubiquitin ligase in complex with ubiquitin. Determined by X-ray diffraction at 1.9 Å resolution. Released 6 Feb 2007.

Method
X-ray diffraction
Resolution
1.9 Å
Organisms
Homo sapiens, Bos taurus
Chains
2
Atoms
1,058
Mol. weight
14.23 kDa
Released
6 Feb 2007

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

Secondary structure: helices and β-sheets

2OOB contains 7 α-helices and 7 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.

Chain A: 3 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix932-94110
α-helix946-95510
α-helix960-97011
Chain B: 4 helices, 7 β-strands
ElementResiduesLengthSheet
β-strand2-651
β-strand12-1651
β-strand2212
α-helix23-3412
α-helix38-403
β-strand41-4551
β-strand48-4921
α-helix50-512
β-strand5512
α-helix57-593
β-strand66-7161

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
E3 ubiquitin-protein ligase CBL-BAprotein52Homo sapiensQ13191 (AlphaFold model)
UbiquitinBprotein76Bos taurusP0CH28 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2OOB_1 E3 ubiquitin-protein ligase CBL-B (chains A)
GSGPEAALENVDAKIAKLMGEGYAFEEVKRALEIAQNNVEVARSILREFAFP
Sequence of entity 2 (B), FASTA
>2OOB_2 Ubiquitin (chains B)
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN
IQKESTLHLVLRLRGG

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:

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