Intersectin-1 (ITSN1) is a 1721-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15811.
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The mean pLDDT of this model is 72.3 (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 | 34% |
| 70 to 90 | Confident: backbone generally right | 33% |
| 50 to 70 | Low: treat with caution | 9% |
| Below 50 | Very low: often disordered regions | 24% |
What pLDDT means and how to read it
Adapter protein that provides a link between the endocytic membrane traffic and the actin assembly machinery (PubMed:11584276, PubMed:29887380). Acts as a guanine nucleotide exchange factor (GEF) for CDC42, and thereby stimulates actin nucleation mediated by WASL and the ARP2/3 complex (PubMed:11584276). Plays a role in the assembly and maturation of clathrin-coated vesicles (By similarity). Recruits FCHSD2 to clathrin-coated pits (PubMed:29887380). Involved in endocytosis of activated EGFR, and probably also other growth factor receptors (By similarity). Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but…
Interacts (via DH domain) with CDC42 (PubMed:11584276, PubMed:12006984). Interacts (via SH3 domain 1) with WASL (PubMed:11584276). Interacts with dynamin, SNAP25 and SNAP23 (By similarity). Interacts with clathrin-associated proteins and other components of the endocytic machinery, such as SPIN90, EPS15, EPN1, EPN2, STON2, FCHO1, FCHO2 and DAB2 (PubMed:20448150, PubMed:22484487,…
Endomembrane system, Synapse, synaptosome, Cell projection, lamellipodium, Cell membrane, Membrane, clathrin-coated pit, Recycling endosome, Endosome, Cytoplasmic vesicle, Cytoplasm, Nucleus envelope
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3FIA | X-ray | 1.45 Å | A=1-111 |
| 6H5T | X-ray | 1.69 Å | A/B=741-840 |
| 4IIM | X-ray | 1.8 Å | A/B=916-970 |
| 1KI1 | X-ray | 2.3 Å | B/D=1229-1581 |
| 5HZI | X-ray | 2.6 Å | A/B=1230-1580 |
| 5HZJ | X-ray | 2.6 Å | A/B=1230-1580 |
| 3QBV | X-ray | 2.65 Å | B/D=1229-1579 |
| 5HZK | X-ray | 3.3 Å | B/D=1230-1580 |
| 6GBU | X-ray | 3.44 Å | B/D/F/H=1074-1138 |
| 2KGR | NMR | A=210-312 | |
| 2KHN | NMR | A=1-111 |
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