2BBU: Mouse socs3

solution structure of mouse socs3 in complex with a phosphopeptide from the gp130 receptor. Determined by solution NMR. Released 2 May 2006.

Method
Solution NMR
Organism
Mus musculus
Chains
2
Atoms
1,316
Mol. weight
19.57 kDa
Released
2 May 2006

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

Secondary structure: helices and β-sheets

2BBU contains 3 α-helices and 7 β-strands across 1 chain. 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, 7 β-strands

ElementResiduesLengthSheet
α-helix2-1413
α-helix24-3310
β-strand40-4341
β-strand51-5551
β-strand62-6541
β-strand67-6932
β-strand72-7432
α-helix90-989
β-strand138-13923
β-strand144-14523

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Suppressor of cytokine signaling 3Aprotein164Mus musculusO35718 (AlphaFold model)
GP130 phosphopeptideBprotein15Q00560 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2BBU_1 Suppressor of cytokine signaling 3 (chains A)
LKTFSSKSEYQLVVNAVRKLQESGFYWSAVTGGEANLLLSAEPAGTFLIRDSSDQRHFFT
LSVKTQSGTKNLRIQCEGGSFSLQSDPRSTQPVPRFDCVLKLVHHYMPPPGTPSFSLPPT
EPSSEVPEQPPAQALPGSTPKRAYYIYSGGEKIPLVLSRPLSSN
Sequence of entity 2 (B), FASTA
>2BBU_2 GP130 PHOSPHOPEPTIDE (chains B)
STASTVEYSTVVHSG

Primary citation

The Structure of SOCS3 Reveals the Basis of the Extended SH2 Domain Function and Identifies an Unstructured Insertion That Regulates Stability. Babon, J.J., McManus, E.J., Yao, S. et al. Mol Cell (2006) 22:205-216. DOI 10.1016/j.molcel.2006.03.024 · PubMed

Other PDB entries of the same protein (UniProt O35718 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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