2GBQ: GRB2 N-terminal SH3 domain

Solution NMR structure of the GRB2 N-terminal SH3 domain complexed with a ten-residue peptide derived from sos direct refinement against noes, J-couplings, and 1H and 13C chemical shifts, 15 structures. Determined by solution NMR. Released 4 Sept 1997.

Method
Solution NMR
Organism
Mus musculus
Chains
2
Atoms
552
Mol. weight
9.65 kDa
Released
4 Sept 1997

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

Secondary structure: helices and β-sheets

2GBQ contains 2 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: 1 helix, 8 β-strands

ElementResiduesLengthSheet
β-strand2-541
β-strand912
β-strand1611
β-strand1912
β-strand24-2741
β-strand36-4161
β-strand44-4961
α-helix50-523
β-strand53-5641
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix2-65

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
GRB2Aprotein74Mus musculusQ60631 (AlphaFold model)
SOS-1Bprotein12Mus musculusQ62245 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2GBQ_1 GRB2 (chains A)
GSRRASVGSMEAIAKYDFKATADDELSFKRGDILKVLNEECDQNWYKAELNGKDGFIPKN
YIEMKPHPEFIVTD
Sequence of entity 2 (B), FASTA
>2GBQ_2 SOS-1 (chains B)
XVPPPVPPRRRX

Primary citation

Solution structure of the Grb2 N-terminal SH3 domain complexed with a ten-residue peptide derived from SOS: direct refinement against NOEs, J-couplings and 1H and 13C chemical shifts. Wittekind, M., Mapelli, C., Lee, V. et al. J Mol Biol (1997) 267:933-952. DOI 10.1006/jmbi.1996.0886 · PubMed

Other PDB entries of the same protein (UniProt Q60631 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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