AP-2 complex subunit mu (Ap2m1) is a 435-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P84092.
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The mean pLDDT of this model is 89.7 (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 | 74% |
| 70 to 90 | Confident: backbone generally right | 19% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 3% |
What pLDDT means and how to read it
Component of the adaptor protein complex 2 (AP-2) (PubMed:14745134, PubMed:15473838). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways (PubMed:14745134, PubMed:15473838). Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation (PubMed:14745134, PubMed:15473838). AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome (PubMed:14745134, PubMed:15473838). The clathrin lattice serves as a mechanical…
Adaptor protein complex 2 (AP-2) is a heterotetramer composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2 and beta-type subunit AP2B1), a medium adaptin (mu-type subunit AP2M1) and a small adaptin (sigma-type subunit AP2S1) (PubMed:19140243). Interacts with ATP6V1H and MEGF10 (By similarity). Interacts with EGFR and TTGN1 (PubMed:10228163, PubMed:12121421, PubMed:9812899). Interacts…
Cell membrane, Membrane, coated pit
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7OIQ | X-ray | 1.85 Å | AAA/BBB=158-435 |
| 7OFP | X-ray | 1.92 Å | A/B=158-435 |
| 7OHZ | X-ray | 2.27 Å | A/B=158-435 |
| 1I31 | X-ray | 2.5 Å | A=122-435 |
| 2PR9 | X-ray | 2.51 Å | A=158-435 |
| 6QH5 | X-ray | 2.56 Å | M/N=1-435 |
| 2VGL | X-ray | 2.59 Å | M=1-435 |
| 3H85 | X-ray | 2.6 Å | A=158-435 |
| 5WRM | X-ray | 2.6 Å | A=158-435 |
| 7OI5 | X-ray | 2.61 Å | B/D=158-435 |
| 5WRK | X-ray | 2.62 Å | A=158-435 |
| 1BW8 | X-ray | 2.65 Å | A=120-435 |
| 1BXX | X-ray | 2.7 Å | A=158-435 |
| 5C7Z | X-ray | 2.77 Å | A=159-435 |
| 5FPI | X-ray | 2.77 Å | A=1-435 |
| 9FIX | X-ray | 2.78 Å | M=158-435 |
| 4UQI | X-ray | 2.79 Å | M=1-435 |
| 2BP5 | X-ray | 2.8 Å | M=1-435 |
| 9FIW | X-ray | 2.82 Å | M=158-435 |
| 7OHO | X-ray | 2.88 Å | MMM=1-435 |
Showing 20 of 37 experimental structures (best resolution first).
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