Tyrosine-protein kinase ABL1 (Abl1) is a 1123-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P00520.
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The mean pLDDT of this model is 63.4 (low 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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 37% |
| 70 to 90 | Confident: backbone generally right | 9% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 49% |
What pLDDT means and how to read it
Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like WASF3 (involved in branch formation); ANXA1 (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); or MAPT and PXN (microtubule-binding proteins). Phosphorylation of WASF3 is critical for the stimulation of lamellipodia formation and cell migration. Involved in the…
Interacts with INPPL1/SHIP2. Interacts with SORBS1 following insulin stimulation. Found in a trimolecular complex containing CDK5 and CABLES1. Interacts with CABLES1 and PSTPIP1. Interacts with ZDHHC16. Interacts with the 14-3-3 proteins, YWHAB, YWHAE, YWHAG, YWHAH, SFN and YWHAZ; the interaction with 14-3-3 proteins requires phosphorylation on Thr-734 and sequesters ABL1 into the cytoplasm.…
Cytoplasm, cytoskeleton, Nucleus, Mitochondrion
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3KFA | X-ray | 1.22 Å | A/B=229-515 |
| 3K5V | X-ray | 1.74 Å | A/B=229-515 |
| 1OPJ | X-ray | 1.75 Å | A/B=229-515 |
| 1OPK | X-ray | 1.8 Å | A=27-515 |
| 3MS9 | X-ray | 1.8 Å | A/B=229-515 |
| 5IH2 | X-ray | 1.8 Å | M/N=757-765 |
| 3IK3 | X-ray | 1.9 Å | A/B=229-513 |
| 3KF4 | X-ray | 1.9 Å | A/B=229-515 |
| 2QOH | X-ray | 1.95 Å | A/B=229-515 |
| 2Z60 | X-ray | 1.95 Å | A=229-515 |
| 3MSS | X-ray | 1.95 Å | A/B/C/D=229-515 |
| 3OY3 | X-ray | 1.95 Å | A/B=229-511 |
| 1ABO | X-ray | 2.0 Å | A/B=61-121 |
| 3DK7 | X-ray | 2.01 Å | A/B=233-505 |
| 3DK3 | X-ray | 2.02 Å | A/B=233-514 |
| 3DK6 | X-ray | 2.02 Å | A/B=233-514 |
| 6HD4 | X-ray | 2.03 Å | A/B=229-515 |
| 1IEP | X-ray | 2.1 Å | A/B=229-515 |
| 3OXZ | X-ray | 2.2 Å | A=229-511 |
| 6HD6 | X-ray | 2.3 Å | A/B=229-515 |
Showing 20 of 24 experimental structures (best resolution first).
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