AP-2 complex subunit beta (AP2B1) is a 937-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P63010.
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The mean pLDDT of this model is 82.6 (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 | 61% |
| 70 to 90 | Confident: backbone generally right | 24% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 12% |
What pLDDT means and how to read it
Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. 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. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly…
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:12086608, PubMed:19140243). Interacts with EPN1 (PubMed:10944104, PubMed:16516836). Interacts with EPS15; clathrin competes with EPS15 (PubMed:10944104,…
Cell membrane, Membrane, coated pit
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2G30 | X-ray | 1.6 Å | A=701-937 |
| 1E42 | X-ray | 1.7 Å | A/B=701-937 |
| 5M5R | X-ray | 1.76 Å | C/D=629-637 |
| 2IV9 | X-ray | 1.9 Å | A/B=700-937 |
| 6QH5 | X-ray | 2.56 Å | B=1-592 |
| 2VGL | X-ray | 2.59 Å | B=1-591 |
| 4UQI | X-ray | 2.79 Å | B=1-651 |
| 2IV8 | X-ray | 2.8 Å | A=700-937 |
| 7OHO | X-ray | 2.88 Å | BBB=1-542 |
| 2JKR | X-ray | 2.98 Å | B/E=1-591 |
| 6URI | X-ray | 3.0 Å | B=1-591 |
| 2XA7 | X-ray | 3.1 Å | B=1-592 |
| 7OG1 | X-ray | 3.25 Å | BBB=1-591 |
| 2JKT | X-ray | 3.4 Å | B/E=1-591 |
| 6QH7 | X-ray | 3.4 Å | B=1-592 |
| 6YAE | EM | 3.9 Å | B=1-591 |
| 7Z5C | EM | 4.16 Å | B=1-591 |
| 6QH6 | X-ray | 5.0 Å | B=1-592 |
| 6YAF | EM | 9.1 Å | B=1-937 |
| 6YAI | EM | 9.2 Å | F=705-937 |
Showing 20 of 22 experimental structures (best resolution first).
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