9EHD: N-SH2 domain of SHP2

Crystal structure of N-SH2 domain of SHP2 bound to GAB1 tyrosine phosphorylated peptide (624-633) QVEpYLDLDLD. Determined by X-ray diffraction at 1.59 Å resolution. Released 7 Jan 2026.

Method
X-ray diffraction
Resolution
1.59 Å
Organism
Homo sapiens
Chains
2
Atoms
945
Mol. weight
13.51 kDa
Released
7 Jan 2026

Explore 9EHD in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9EHD contains 2 α-helices and 12 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: 2 helices, 11 β-strands

ElementResiduesLengthSheet
β-strand711
α-helix13-2311
β-strand28-3361
β-strand41-4771
β-strand50-5671
β-strand57-5822
β-strand63-6422
β-strand7112
α-helix74-8310
β-strand8913
β-strand9014
β-strand9513
β-strand100-10121
Chain B: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand814

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Isoform 1 of Tyrosine-protein phosphatase non-receptor type 11Aprotein109Homo sapiensQ06124 (AlphaFold model)
Phosphorylated peptide from GRB2-associated-binding protein 1Bprotein10Homo sapiensQ13480 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9EHD_1 Isoform 1 of Tyrosine-protein phosphatase non-receptor type 11 (chains A)
GSGMTSRRWFHPNITGVEAENLLLTRGVDGSFLARPSKSNPGDFTLSVRRNGAVTHIKIQ
NTGDYYDLYGGEKFATLAELVQYYMEHHGQLKEKNGDVIELKYPLNCAD
Sequence of entity 2 (B), FASTA
>9EHD_2 Phosphorylated peptide from GRB2-associated-binding protein 1 (chains B)
QVEYLDLDLD

Primary citation

Phosphatase SHP2 pathogenic mutations enhance activity by altering conformational sampling. Glaser, A.W., Padua, R.A.P., Ojoawo, A.M. et al. Proc Natl Acad Sci U S A (2026) 123:e2513851123-e2513851123. DOI 10.1073/pnas.2513851123 · PubMed

Other PDB entries of the same protein (UniProt Q06124 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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