1RPY: Dimeric SH2 domain of aps

Crystal structure of the dimeric SH2 domain of aps. Determined by X-ray diffraction at 2.3 Å resolution. Released 23 Dec 2003.

Method
X-ray diffraction
Resolution
2.3 Å
Organism
Rattus norvegicus
Chains
2
Atoms
1,400
Mol. weight
26.07 kDa
Released
23 Dec 2003

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

Secondary structure: helices and β-sheets

1RPY contains 8 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: 4 helices, 4 β-strands

ElementResiduesLengthSheet
α-helix404-4063
β-strand41011
α-helix416-4249
α-helix427-4304
β-strand434-43851
β-strand446-45271
β-strand455-46061
α-helix469-48618
Chain B: 4 helices, 4 β-strands
ElementResiduesLengthSheet
β-strand41012
α-helix416-4249
α-helix427-4304
β-strand434-43852
β-strand446-45272
β-strand455-46172
α-helix469-48618
α-helix490-4923

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
adaptor protein APSA, Bprotein114Rattus norvegicusQ9Z200 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1RPY_1 adaptor protein APS (chains A, B)
GSHMELELSDYPWFHGTLSRVKAAQLVLAGGPRSHGLFVIRQSETRPGECVLTFNFQGKA
KHLRLSLNGHGQCHVQHLWFQSVFDMLRHFHTHPIPLESGGSADITLRSYVRAQ

Primary citation

Structural basis for recruitment of the adaptor protein APS to the activated insulin receptor. Hu, J., Liu, J., Ghirlando, R. et al. Mol Cell (2003) 12:1379-1389. DOI 10.1016/S1097-2765(03)00487-8 · PubMed

Other PDB entries of the same protein (UniProt Q9Z200 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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