Scaffold protein ILK (ILK) is a 452-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13418.
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The mean pLDDT of this model is 88.2 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 63% |
| 70 to 90 | Confident: backbone generally right | 30% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
Scaffold protein which mediates protein-protein interactions during a range of cellular events including focal adhesion assembly, cell adhesion and cell migration (PubMed:17420447, PubMed:20005845, PubMed:30367047, PubMed:32528174). Regulates integrin-mediated signal transduction by contributing to inside-out integrin activation (By similarity). Recruits PARVA and LIMS1/PITCH to form the heterotrimeric IPP (ILK-PINCH-PARVIN) complex which binds to F-actin via the C-terminal tail of LIMS1 and the N-terminal region of PARVA, promoting F-actin filament bundling, a process required to generate force for actin cytoskeleton reorganization and subsequent dynamic cell adhesion events such as cell…
Component of the heterotrimeric IPP (ILK-PINCH-PARVIN) complex composed of ILK, LIMS1/PINCH and PARVA; the complex binds to F-actin via the C-terminal tail of LIMS1 and the N-terminal region of PARVA, promoting F-actin filament bundling (PubMed:11331308, PubMed:12167643, PubMed:12432066, PubMed:19074270, PubMed:19117955, PubMed:21524996, PubMed:30367047, PubMed:35259013). Formation of the IPP…
Cell junction, focal adhesion, Cell membrane, Cell projection, lamellipodium, Cytoplasm, myofibril, sarcomere, Cytoplasm, Nucleus, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Cytoplasm, cell cortex
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4HI8 | X-ray | 1.2 Å | A=1-174 |
| 4HI9 | X-ray | 1.2 Å | A=1-174 |
| 9D5E | X-ray | 1.5 Å | A=182-452 |
| 9D5F | X-ray | 1.5 Å | A=182-452 |
| 9D5H | X-ray | 1.5 Å | A=182-452 |
| 9D5I | X-ray | 1.5 Å | A=182-452 |
| 9D5P | X-ray | 1.5 Å | A=182-452 |
| 9D5G | X-ray | 1.55 Å | AAAA=182-452 |
| 3F6Q | X-ray | 1.6 Å | A=1-174 |
| 3KMU | X-ray | 1.8 Å | A=183-452 |
| 3REP | X-ray | 1.8 Å | A=182-452 |
| 6MIB | X-ray | 1.8 Å | A=182-452 |
| 3IXE | X-ray | 1.9 Å | A=1-174 |
| 3KMW | X-ray | 2.0 Å | A=183-452 |
| 2KBX | NMR | A=1-171 |
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