Integrin beta-2 (ITGB2) is a 769-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P05107.
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The mean pLDDT of this model is 85.8 (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 | 51% |
| 70 to 90 | Confident: backbone generally right | 39% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
Integrin ITGAL:ITGB2 is a receptor for ICAM1, ICAM2 and ICAM3 (PubMed:1676048, PubMed:23775590, PubMed:38195629). Integrin ITGAL:ITGB2 is also a receptor for the secreted form of ubiquitin-like protein ISG15; the interaction is mediated by ITGAL (PubMed:29100055). Integrins ITGAM:ITGB2 and ITGAX:ITGB2 are receptors for the iC3b fragment of the third complement component and for fibrinogen. Integrin ITGAX:ITGB2 recognizes the sequence G-P-R in fibrinogen alpha-chain. Integrin ITGAM:ITGB2 recognizes P1 and P2 peptides of fibrinogen gamma chain. Integrin ITGAM:ITGB2 is also a receptor for factor X. Integrin ITGAD:ITGB2 is a receptor for ICAM3 and VCAM1 (PubMed:10438935, PubMed:8777714,…
Heterodimer of an alpha and a beta subunit (PubMed:20033057, PubMed:26936951). The ITGB2 beta subunit associates with the ITGAL, ITGAM, ITGAX or ITGAD alpha subunits (PubMed:20033057, PubMed:24385486, PubMed:26936951). Found in a complex with CD177 and ITGAM/CD11b (PubMed:21193407, PubMed:28807980). Interacts with FGR (By similarity). Interacts with COPS5 and RANBP9 (PubMed:10766246,…
Cell membrane, Membrane raft
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2P26 | X-ray | 1.75 Å | A=23-535 |
| 5E6X | X-ray | 1.75 Å | A=23-535 |
| 1YUK | X-ray | 1.8 Å | A=23-125, B=365-482 |
| 5E6V | X-ray | 1.8 Å | A=23-482 |
| 5E6S | X-ray | 2.15 Å | B/D/F=23-482 |
| 2JF1 | X-ray | 2.2 Å | T=735-769 |
| 2P28 | X-ray | 2.2 Å | A=23-122, B=362-574 |
| 5E6W | X-ray | 2.2 Å | A=23-118, A=362-574 |
| 2V7D | X-ray | 2.5 Å | P/Q/R/S=755-764 |
| 5E6U | X-ray | 2.5 Å | B=23-482 |
| 9RM9 | EM | 2.6 Å | B=23-482 |
| 7USL | EM | 2.7 Å | B=23-699 |
| 7USM | EM | 2.7 Å | B=23-699 |
| 9T5W | EM | 2.74 Å | B=23-482 |
| 4NEH | X-ray | 2.75 Å | B=23-696 |
| 4NEN | X-ray | 2.9 Å | B=23-696 |
| 5E6R | X-ray | 2.9 Å | B=23-482 |
| 9T5V | EM | 3.06 Å | B=23-485 |
| 9T5Z | EM | 3.1 Å | B=23-485 |
| 7P2D | X-ray | 3.2 Å | B=23-482 |
Showing 20 of 29 experimental structures (best resolution first).
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