3OB2: C-Cbl TKB domain

Crystal structure of c-Cbl TKB domain in complex with double phosphorylated EGFR peptide. Determined by X-ray diffraction at 2.1 Å resolution. Released 18 Aug 2010.

Method
X-ray diffraction
Resolution
2.1 Å
Organism
Homo sapiens
Chains
2
Atoms
2,848
Mol. weight
39.77 kDa
Released
18 Aug 2010

Explore 3OB2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3OB2 contains 18 α-helices and 8 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: 0 helices, 1 β-strand

ElementResiduesLengthSheet
β-strand107011
Chain B: 18 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix56-7015
α-helix73-753
α-helix84-10118
α-helix106-1116
α-helix113-13624
α-helix137-1404
α-helix146-16823
α-helix170-1723
α-helix176-1783
α-helix184-19411
β-strand199-20132
α-helix202-21211
α-helix218-22811
β-strand235-23732
α-helix238-24710
α-helix251-2533
α-helix254-2585
α-helix259-2635
β-strand26811
α-helix274-2829
β-strand290-29561
β-strand303-30861
β-strand314-31741
α-helix324-33310
β-strand339-34021

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
12-meric peptide from Epidermal growth factor receptorAprotein12Homo sapiensP00533 (AlphaFold model)
E3 ubiquitin-protein ligase CBLBprotein329Homo sapiensP22681 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3OB2_1 12-meric peptide from Epidermal growth factor receptor (chains A)
DSFLQRYSSDPT
Sequence of entity 2 (B), FASTA
>3OB2_2 E3 ubiquitin-protein ligase CBL (chains B)
GSLIGLMKDAFQPHHHHHHHLSPHPPGTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPP
YILDLLPDTYQHLRTILSRYEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYE
ENSQPRRNLTKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGEKTIVPW
KSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWSSLLRNWNSLA
VTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLSCTRLGQWAIGYVTADGNILQTIPHNK
PLFQALIDGFREGFYLFPDGRNQNPDLTG

Primary citation

Additional serine/threonine phosphorylation reduces binding affinity but preserves interface topography of substrate proteins to the c-Cbl TKB domain. Sun, Q., Jackson, R.A., Ng, C. et al. PLoS One (2010) 5:e12819-e12819. DOI 10.1371/journal.pone.0012819 · PubMed

Other PDB entries of the same protein (UniProt P00533 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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