P06239: Tyrosine-protein kinase Lck (LCK)

Tyrosine-protein kinase Lck (LCK) is a 509-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P06239.

Gene
LCK
Organism
Homo sapiens
Length
509 residues
Mean pLDDT
83.6
Model
AF-P06239-F1 v6
Model created
1 Aug 2025
PDB structures
57

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Model confidence (pLDDT)

The mean pLDDT of this model is 83.6 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate61%
70 to 90Confident: backbone generally right22%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions12%

What pLDDT means and how to read it

Function

Non-receptor tyrosine-protein kinase that plays an essential role in the selection and maturation of developing T-cells in the thymus and in the function of mature T-cells (PubMed:2470098). Plays a key role in T-cell antigen receptor (TCR)-linked signal transduction pathways (PubMed:2470098). Constitutively associated with the cytoplasmic portions of the CD4 and CD8 surface receptors (PubMed:2470098). Association of the TCR with a peptide antigen-bound MHC complex facilitates the interaction of CD4 and CD8 with MHC class II and class I molecules, respectively, thereby recruiting the associated LCK protein to the vicinity of the TCR-CD3 complex (PubMed:2470098). LCK then phosphorylates…

Subunit structure

Binds to the cytoplasmic domain of cell surface receptors, such as AXL, CD2, CD4, CD5, CD8, CD44, CD45 and CD122. Also binds to effector molecules, such as PI4K, VAV1, RASA1, FYB1 and to other protein kinases including CDK1, RAF1, ZAP70 and SYK. Binds to phosphatidylinositol 3'-kinase (PI3K) from T-lymphocytes through its SH3 domain and to the tyrosine phosphorylated form of KHDRBS1/p70 through…

Subcellular location

Cell membrane, Cytoplasm, cytosol

Disease associations

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
1LKKX-ray1.0 ÅA=122-226
2IIMX-ray1.0 ÅA=59-119
8X2PX-ray1.4 ÅA/B=119-226
1QPCX-ray1.6 ÅA=231-509
3LCKX-ray1.7 ÅA=231-501
4C3FX-ray1.72 ÅA=237-501
1BHFX-ray1.8 ÅA=119-226
1LCJX-ray1.8 ÅA=119-226
1LKLX-ray1.8 ÅA=123-226
6PDJX-ray1.81 ÅA=225-509
1BHHX-ray1.9 ÅA=119-226, B=124-226
3MPMX-ray1.95 ÅA=237-501
3AC1X-ray1.99 ÅA=225-509
1QPDX-ray2.0 ÅA=231-509
1QPEX-ray2.0 ÅA=231-509
2OF2X-ray2.0 ÅA=231-501
2OFUX-ray2.0 ÅA=229-501
2OFVX-ray2.0 ÅA/B=232-498
3AD5X-ray2.0 ÅA=225-509
3BYMX-ray2.0 ÅA=230-501

Showing 20 of 57 experimental structures (best resolution first).

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