Integrin alpha-M (ITGAM) is a 1152-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P11215.
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The mean pLDDT of this model is 86.3 (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 | 40% |
| 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 ITGAM/ITGB2 is implicated in various adhesive interactions of monocytes, macrophages and granulocytes as well as in mediating the uptake of complement-coated particles and pathogens (PubMed:20008295, PubMed:9558116). It is identical with CR-3, the receptor for the iC3b fragment of the third complement component. It probably recognizes the R-G-D peptide in C3b. Integrin ITGAM/ITGB2 is also a receptor for fibrinogen and factor X. It recognizes P1 and P2 peptides of fibrinogen gamma chain. Regulates neutrophil migration (PubMed:28807980). In association with beta subunit ITGB2/CD18, required for CD177-PRTN3-mediated activation of TNF primed neutrophils (PubMed:21193407). Integrin…
Heterodimer of an alpha and a beta subunit. ITGAM associates with ITGB2 (Probable). Found in a complex with CD177 and ITGB2/CD18 (PubMed:21193407). Interacts with JAM3 (PubMed:12208882, PubMed:15194813). Interacts with THBD (PubMed:27055590). Interacts with complement factor H/CFH; this interaction mediates adhesion of neutrophils to pathogens leading to pathogen clearance (PubMed:20008295,…
Cell membrane, Membrane raft
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1MF7 | X-ray | 1.25 Å | A=144-335 |
| 1NA5 | X-ray | 1.5 Å | A=144-335 |
| 8CE6 | X-ray | 1.58 Å | A=149-337 |
| 1IDO | X-ray | 1.7 Å | A=143-331 |
| 1JLM | X-ray | 2.0 Å | A=143-334 |
| 4XW2 | X-ray | 2.0 Å | A=145-337 |
| 8CE9 | X-ray | 2.11 Å | A/B=149-337 |
| 1M1U | X-ray | 2.3 Å | A=139-331 |
| 1N9Z | X-ray | 2.5 Å | A=144-335 |
| 9RM9 | EM | 2.6 Å | A=17-769 |
| 1BHO | X-ray | 2.7 Å | 1/2=149-337 |
| 1BHQ | X-ray | 2.7 Å | 1/2=149-337 |
| 1IDN | X-ray | 2.7 Å | 1/2=149-337 |
| 3Q3G | X-ray | 2.7 Å | E/G/I/L=148-337 |
| 7USL | EM | 2.7 Å | A=17-1104 |
| 7USM | EM | 2.7 Å | A=17-1104 |
| 9T5W | EM | 2.74 Å | A=17-769 |
| 6RHW | X-ray | 2.75 Å | C=143-337 |
| 4M76 | X-ray | 2.8 Å | B=143-337 |
| 3QA3 | X-ray | 3.0 Å | E/G/I/L=148-337 |
Showing 20 of 31 experimental structures (best resolution first).
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