Matrix protein 1 (M) is a 252-residue protein from Influenza A virus. This is its AlphaFold structure prediction, created 3 Jul 2025. UniProt accession: P03485.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 79.9 (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 | 42% |
| 70 to 90 | Confident: backbone generally right | 31% |
| 50 to 70 | Low: treat with caution | 21% |
| Below 50 | Very low: often disordered regions | 5% |
What pLDDT means and how to read it
Plays critical roles in virus replication, from virus entry and uncoating to assembly and budding of the virus particle. M1 binding to ribonucleocapsids (RNPs) in nucleus seems to inhibit viral transcription. Interaction of viral NEP with M1-RNP is thought to promote nuclear export of the complex, which is targeted to the virion assembly site at the apical plasma membrane in polarized epithelial cells. Interactions with NA and HA may bring M1, a non-raft-associated protein, into lipid rafts. Forms a continuous shell on the inner side of the lipid bilayer in virion, where it binds the RNP. During virus entry into cell, the M2 ion channel acidifies the internal virion core, inducing M1…
Homodimer and homomultimer. Interacts with NEP (PubMed:8356796). Binds ribonucleocapsid by both interacting with genomic RNA and NP protein (PubMed:11222100). May interact with HA and NA. Cannot bind NP without genomic RNA (PubMed:11222100). Interacts with human STING (PubMed:41747053)
Virion membrane, Host nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2VLL | X-ray | 1.6 Å | C/F=58-66 |
| 5TEZ | X-ray | 1.7 Å | C=58-66 |
| 5ISZ | X-ray | 2.06 Å | C=58-66 |
| 1AA7 | X-ray | 2.08 Å | A/B=1-158 |
| 5CQE | X-ray | 2.1 Å | A/B=1-164 |
| 5EUO | X-ray | 2.1 Å | I/J=58-66 |
| 1EA3 | X-ray | 2.3 Å | A/B=1-164 |
| 2VLR | X-ray | 2.3 Å | C/H=58-66 |
| 5JHD | X-ray | 2.46 Å | C/H=58-66 |
| 1HHI | X-ray | 2.5 Å | C/F=58-66 |
| 3VDX | X-ray | 3.0 Å | A/B/C=3-164 |
| 7JM3 | EM | 3.4 Å | C=2-252 |
| 4IQ4 | X-ray | 3.5 Å | A/B/C/D/E/F=3-164 |
| 4ITV | X-ray | 3.6 Å | A/B/C/D/E/F/G/H/I/J/K/L=3-164 |
| 6Z5L | EM | 3.8 Å | A=1-252 |
| 4D9J | X-ray | 3.92 Å | A/B/C/D/E/F/G/H/I/J/K/L=3-164 |
| 5E6I | X-ray | 4.0 Å | E/K/O/T=58-66 |
| 4QES | X-ray | 4.19 Å | A/B/C=3-164 |
| 4QF0 | X-ray | 6.49 Å | A/B/C/D/E/F=3-164 |
| 4IVJ | X-ray | 7.35 Å | A/B/C=3-164 |
Showing 20 of 21 experimental structures (best resolution first).
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