Integrin alpha-L (ITGAL) is a 1170-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P20701.
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The mean pLDDT of this model is 82.6 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 42% |
| 70 to 90 | Confident: backbone generally right | 41% |
| 50 to 70 | Low: treat with caution | 9% |
| Below 50 | Very low: often disordered regions | 8% |
What pLDDT means and how to read it
Integrin ITGAL/ITGB2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4 (PubMed:10846180, PubMed:12526797, PubMed:1676048, PubMed:3086451). Integrin ITGAL/ITGB2 is a receptor for F11R (PubMed:11812992, PubMed:15528364). Integrin ITGAL/ITGB2 is a receptor for the secreted form of ubiquitin-like protein ISG15; the interaction is mediated by ITGAL (PubMed:29100055). Involved in a variety of immune phenomena including leukocyte-endothelial cell interaction, cytotoxic T-cell mediated killing, and antibody dependent killing by granulocytes and monocytes. Contributes to natural killer cell cytotoxicity (PubMed:15356110). Involved in leukocyte adhesion and transmigration of leukocytes including…
Heterodimer of an alpha and a beta subunit (PubMed:12526797). The ITGAL alpha subunit associates with the ITGB2 beta subunit (PubMed:12526797). Interacts with THBD (PubMed:27055590). Interacts with CD226 (PubMed:15684041, PubMed:38195629)
Cell membrane, Membrane raft
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1MJN | X-ray | 1.3 Å | A=153-331 |
| 2ICA | X-ray | 1.56 Å | A=154-332 |
| 3F78 | X-ray | 1.6 Å | A/B/C=153-332 |
| 1T0P | X-ray | 1.66 Å | A=153-326 |
| 3F74 | X-ray | 1.7 Å | A/B/C=153-332 |
| 2O7N | X-ray | 1.75 Å | A=154-332 |
| 1LFA | X-ray | 1.8 Å | A/B=150-336 |
| 1XUO | X-ray | 1.8 Å | A/B=152-336 |
| 3BQN | X-ray | 1.8 Å | B/C=153-334 |
| 4IXD | X-ray | 1.8 Å | A=152-336 |
| 7KC3 | X-ray | 1.8 Å | C=149-341 |
| 3M6F | X-ray | 1.85 Å | A=154-332 |
| 7KC6 | X-ray | 1.85 Å | A/C=153-334 |
| 7KC5 | X-ray | 1.86 Å | A/C=153-334 |
| 3BQM | X-ray | 1.95 Å | B/C=153-334 |
| 1MQ9 | X-ray | 2.0 Å | A=153-331 |
| 1ZON | X-ray | 2.0 Å | A=150-336 |
| 1ZOP | X-ray | 2.0 Å | A/B=150-336 |
| 3E2M | X-ray | 2.0 Å | A/B=152-334 |
| 6BXJ | X-ray | 2.09 Å | A=153-331 |
Showing 20 of 41 experimental structures (best resolution first).
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