1LCJ: P56==LCK== tyrosine kinase

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.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Homo sapiens
Chains
2
Atoms
1,002
Mol. weight
13.86 kDa
Released
15 Oct 1995

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

Secondary structure: helices and β-sheets

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.

Chain A: 2 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand12811
α-helix134-1418
β-strand151-15551
β-strand163-17191
β-strand175-18391
β-strand184-18632
β-strand190-19232
β-strand19912
α-helix202-21110
β-strand22311
Chain B: 1 helix, 1 β-strand
ElementResiduesLengthSheet
β-strand20511
α-helix207-2104

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
P56==LCK== tyrosine kinaseAprotein109Homo sapiensP06239 (AlphaFold model)
Phosphopeptide epq(phospho)yeeipiylBprotein11P03079
Sequence of entity 1 (A), FASTA
>1LCJ_1 P56==LCK== TYROSINE KINASE (chains A)
MANSLEPEPWFFKNLSRKDAERQLLAPGNTHGSFLIRESESTAGSFSLSVRDFDQNQGEV
VKHYKIRNLDNGGFYISPRITFPGLHELVRHYTNASDGLCTRLSRPCQT
Sequence of entity 2 (B), FASTA
>1LCJ_2 PHOSPHOPEPTIDE EPQ(PHOSPHO)YEEIPIYL (chains B)
EPQYEEIPIYL

Primary citation

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:

Browse structure collections

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