Integrin beta-1 (ITGB1) is a 798-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P05556.
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The mean pLDDT of this model is 85.9 (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 | 49% |
| 70 to 90 | Confident: backbone generally right | 40% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 3% |
What pLDDT means and how to read it
Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-4/beta-1 recognizes one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1 are receptors for lamimin. Integrin alpha-6/beta-1…
Heterodimer of an alpha and a beta subunit (PubMed:33962943). Beta-1 associates with either alpha-1, alpha-2, alpha-3, alpha-4, alpha-5, alpha-6, alpha-7, alpha-8, alpha-9, alpha-10, alpha-11 or alpha-V. ITGA6:ITGB1 is found in a complex with CD9; interaction takes place in oocytes and is involved in sperm-egg fusion (By similarity). Interacts with seprase FAP (seprase); the interaction occurs…
Cell membrane, Cell projection, invadopodium membrane, Cell projection, ruffle membrane, Recycling endosome, Melanosome, Cleavage furrow, Cell projection, lamellipodium, Cell junction, focal adhesion, Cell membrane, sarcolemma, Cell junction
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4WK0 | X-ray | 1.78 Å | B=21-465 |
| 4WJK | X-ray | 1.85 Å | B=21-465 |
| 3G9W | X-ray | 2.17 Å | C/D=752-795 |
| 3T9K | X-ray | 2.3 Å | A/B=758-769 |
| 8W30 | X-ray | 2.45 Å | B=21-465 |
| 4WK2 | X-ray | 2.5 Å | B=21-465 |
| 4WK4 | X-ray | 2.5 Å | B=21-465 |
| 9NAB | EM | 2.54 Å | A=21-465 |
| 9B9J | EM | 2.6 Å | B=1-728 |
| 9P6S | EM | 2.61 Å | B=26-465 |
| 9B9K | EM | 2.7 Å | B=1-728 |
| 7CEB | X-ray | 2.89 Å | B=21-465 |
| 3VI3 | X-ray | 2.9 Å | B/D=21-465 |
| 3VI4 | X-ray | 2.9 Å | B/D=21-465 |
| 9DIA | EM | 2.97 Å | B=1-728 |
| 4DX9 | X-ray | 3.0 Å | 6/7/8/9/B/D/F/H/J/L/N/P/R/T/V/X/Z/b/d/f/h/j/l/n/p/r/t/v/x/z=784-798 |
| 7NWL | EM | 3.1 Å | B=21-798 |
| 9CKV | EM | 3.19 Å | B=1-728 |
| 9EF2 | EM | 3.36 Å | B=1-728 |
| 7CEC | EM | 3.9 Å | B=21-465 |
Showing 20 of 22 experimental structures (best resolution first).
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