9EHA: N-SH2 domain of SHP2

Crystal structure of N-SH2 domain of SHP2 bound to phosphotyrosine. Determined by X-ray diffraction at 1.71 Å resolution. Released 7 Jan 2026.

Method
X-ray diffraction
Resolution
1.71 Å
Organism
Homo sapiens
Chains
1
Atoms
913
Mol. weight
12.56 kDa
Ligands
PTR
Released
7 Jan 2026

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

Secondary structure: helices and β-sheets

9EHA contains 2 α-helices 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: 2 helices, 10 β-strands

ElementResiduesLengthSheet
β-strand711
α-helix13-2311
β-strand28-3361
β-strand41-4771
β-strand50-5561
β-strand57-5822
β-strand63-6422
β-strand7112
α-helix74-8310
β-strand8913
β-strand9513
β-strand100-10121

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Isoform 1 of Tyrosine-protein phosphatase non-receptor type 11Aprotein109Homo sapiensQ06124 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9EHA_1 Isoform 1 of Tyrosine-protein phosphatase non-receptor type 11 (chains A)
GSGMTSRRWFHPNITGVEAENLLLTRGVDGSFLARPSKSNPGDFTLSVRRNGAVTHIKIQ
NTGDYYDLYGGEKFATLAELVQYYMEHHGQLKEKNGDVIELKYPLNCAD

Ligands and cofactors

IDNameFormulaCopies
PTRO-phosphotyrosineC9 H12 N O6 P1

Water and common crystallization additives (SO4) are not listed.

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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