1GBR: Growth factor receptor-bound protein 2

Orientation of peptide fragments from sos proteins bound to the N-terminal SH3 domain of GRB2 determined by NMR spectroscopy. Determined by solution NMR. Released 26 Jan 1995.

Method
Solution NMR
Organism
Mus musculus
Chains
2
Atoms
719
Mol. weight
10.23 kDa
Released
26 Jan 1995

Explore 1GBR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1GBR contains 1 α-helix and 10 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: 1 helix, 10 β-strands

ElementResiduesLengthSheet
β-strand1-331
β-strand512
β-strand913
β-strand1611
β-strand1913
β-strand25-2951
β-strand36-4271
β-strand44-4961
α-helix50-523
β-strand5312
β-strand5611

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Growth factor receptor-bound protein 2Aprotein74Mus musculusQ60631 (AlphaFold model)
Sos-a peptideBprotein15Mus musculusQ02384 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1GBR_1 GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2 (chains A)
GSRRASVGSMEAIAKYDFKATADDELSFKRGDILKVLNEECDQNWYKAELNGKDGFIPKN
YIEMKPHPEFIVTD
Sequence of entity 2 (B), FASTA
>1GBR_2 SOS-A PEPTIDE (chains B)
SPLLPKLPPKTYKRE

Primary citation

Orientation of peptide fragments from Sos proteins bound to the N-terminal SH3 domain of Grb2 determined by NMR spectroscopy. Wittekind, M., Mapelli, C., Farmer 2nd., B.T. et al. Biochemistry (1994) 33:13531-13539. DOI 10.1021/bi00250a004 · PubMed

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

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