SH2 (src homology-2) domain of human P56-lck tyrosine kinase complexed with the 11 residue phosphotyrosyl peptide epqpyeeipiyl. Determined by X-ray diffraction at 1.8 Å resolution. Released 15 Oct 1995.
Explore 1LCJ in 3D Show helices and sheets RCSB PDB PDBe
1LCJ contains 3 α-helices and 9 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 128 | 1 | 1 |
| α-helix | 134-141 | 8 | |
| β-strand | 151-155 | 5 | 1 |
| β-strand | 163-171 | 9 | 1 |
| β-strand | 175-183 | 9 | 1 |
| β-strand | 184-186 | 3 | 2 |
| β-strand | 190-192 | 3 | 2 |
| β-strand | 199 | 1 | 2 |
| α-helix | 202-211 | 10 | |
| β-strand | 223 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 205 | 1 | 1 |
| α-helix | 207-210 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| P56==LCK== tyrosine kinase | A | protein | 109 | Homo sapiens | P06239 (AlphaFold model) |
| Phosphopeptide epq(phospho)yeeipiyl | B | protein | 11 | P03079 |
>1LCJ_1 P56==LCK== TYROSINE KINASE (chains A) MANSLEPEPWFFKNLSRKDAERQLLAPGNTHGSFLIRESESTAGSFSLSVRDFDQNQGEV VKHYKIRNLDNGGFYISPRITFPGLHELVRHYTNASDGLCTRLSRPCQT
>1LCJ_2 PHOSPHOPEPTIDE EPQ(PHOSPHO)YEEIPIYL (chains B) EPQYEEIPIYL
Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck. Eck, M.J., Shoelson, S.E., Harrison, S.C. Nature (1993) 362:87-91. DOI 10.1038/362087a0 · PubMed
Other PDB entries of the same protein (UniProt P06239 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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