Gads SH2 domain/CD28-derived peptide complex. Determined by X-ray diffraction at 1.2 Å resolution. Released 14 Dec 2016.
Explore 5GJH in 3D Show helices and sheets RCSB PDB PDBe
5GJH contains 4 α-helices and 18 β-strands across 3 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 59 | 1 | 1 |
| α-helix | 65-73 | 9 | |
| β-strand | 80-84 | 5 | 1 |
| β-strand | 92-97 | 6 | 1 |
| β-strand | 102-107 | 6 | 1 |
| β-strand | 108-109 | 2 | 2 |
| β-strand | 115-116 | 2 | 2 |
| β-strand | 121-122 | 2 | 2 |
| α-helix | 125-134 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 59 | 1 | 3 |
| α-helix | 65-73 | 9 | |
| β-strand | 79 | 1 | 4 |
| β-strand | 80-84 | 5 | 3 |
| β-strand | 92-97 | 6 | 3 |
| β-strand | 102-107 | 6 | 3 |
| β-strand | 108-109 | 2 | 5 |
| β-strand | 115-116 | 2 | 5 |
| β-strand | 121-122 | 2 | 5 |
| α-helix | 125-134 | 10 | |
| β-strand | 146 | 1 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 191 | 1 | 6 |
| β-strand | 194 | 1 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| GRB2-related adapter protein 2 | A, C | protein | 100 | Homo sapiens | O75791 (AlphaFold model) |
| T-cell-specific surface glycoprotein CD28 | B, D | protein | 8 | Homo sapiens | P10747 (AlphaFold model) |
>5GJH_1 GRB2-related adapter protein 2 (chains A, C) GSWFHEGLSRHQAENLLMGKEVGFFIIRASQSSPGDFSISVRHEDDVQHFKVMRDNKGNY FLWTEKFPSLNKLVDYYRTNSISRQKQIFLRDRTREDQGH
>5GJH_2 T-cell-specific surface glycoprotein CD28 (chains B, D) SDYMNMTP
Crystal Structures and Thermodynamic Analysis Reveal Distinct Mechanisms of CD28 Phosphopeptide Binding to the Src Homology 2 (SH2) Domains of Three Adaptor Proteins. Inaba, S., Numoto, N., Ogawa, S. et al. J Biol Chem (2017) 292:1052-1060. DOI 10.1074/jbc.M116.755173 · PubMed
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