1LKK: Human P56-lck tyrosine kinase SH2 domain

Human P56-lck tyrosine kinase SH2 domain in complex with the phosphotyrosyl peptide ac-ptyr-glu-glu-ile (pyeei peptide). Determined by X-ray diffraction at 1.0 Å resolution. Released 8 Mar 1996.

Method
X-ray diffraction
Resolution
1.0 Å
Organism
Homo sapiens
Chains
2
Atoms
1,103
Mol. weight
12.69 kDa
Ligands
ACE
Released
8 Mar 1996

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

Secondary structure: helices and β-sheets

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

ElementResiduesLengthSheet
β-strand12811
α-helix134-1418
β-strand151-15551
β-strand163-17191
β-strand175-18391
β-strand184-18522
α-helix1861
β-strand191-19222
β-strand19912
α-helix202-21110
β-strand22311
α-helix224-2252
Chain B: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand25311

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Human P56 tyrosine kinaseAprotein105Homo sapiensP06239 (AlphaFold model)
Phosphotyrosyl peptide ac-ptyr-glu-glu-ileBprotein5
Sequence of entity 1 (A), FASTA
>1LKK_1 HUMAN P56 TYROSINE KINASE (chains A)
LEPEPWFFKNLSRKDAERQLLAPGNTHGSFLIRESESTAGSFSLSVRDFDQNQGEVVKHY
KIRNLDNGGFYISPRITFPGLHELVRHYTNASDGLCTRLSRPCQT
Sequence of entity 2 (B), FASTA
>1LKK_2 PHOSPHOTYROSYL PEPTIDE AC-PTYR-GLU-GLU-ILE (chains B)
XYEEI

Ligands and cofactors

IDNameFormulaCopies
ACEAcetyl groupC2 H4 O1

Primary citation

Crystal structures of the human p56lck SH2 domain in complex with two short phosphotyrosyl peptides at 1.0 A and 1.8 A resolution. Tong, L., Warren, T.C., King, J. et al. J Mol Biol (1996) 256:601-610. DOI 10.1006/jmbi.1996.0112 · 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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