Receptor tyrosine-protein kinase erbB-2 (ERBB2) is a 1255-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P04626.
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The mean pLDDT of this model is 74.0 (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 | 25% |
| 50 to 70 | Low: treat with caution | 9% |
| Below 50 | Very low: often disordered regions | 25% |
What pLDDT means and how to read it
Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which…
Homodimer (PubMed:21454582). Heterodimer with EGFR, ERBB3 and ERBB4 (PubMed:10358079, PubMed:15093539, PubMed:16978839, PubMed:21190959). Part of a complex with EGFR and either PIK3C2A or PIK3C2B. May interact with PIK3C2B when phosphorylated on Tyr-1196 (PubMed:10805725). Interacts with PLXNB1 (PubMed:15210733). Interacts (when phosphorylated on Tyr-1248) with MEMO1 (PubMed:15156151). Interacts…
Cell membrane, Cell projection, ruffle membrane, Early endosome, Cytoplasm, perinuclear region, Nucleus, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1MFG | X-ray | 1.25 Å | B=1247-1255 |
| 8VB5 | X-ray | 1.48 Å | A=703-1029 |
| 8JYR | X-ray | 1.69 Å | A=23-216 |
| 8U8X | X-ray | 1.69 Å | A=694-1029 |
| 8JYQ | X-ray | 1.75 Å | C/F=611-618 |
| 7PCD | X-ray | 1.77 Å | A=703-1029 |
| 1MFL | X-ray | 1.88 Å | B=1247-1255 |
| 5TQS | X-ray | 1.88 Å | E/F/G/H=1218-1228 |
| 4GFU | X-ray | 2.0 Å | F=1246-1252 |
| 6LBX | X-ray | 2.03 Å | B=531-626 |
| 9IUT | X-ray | 2.09 Å | C/F=611-618 |
| 3PP0 | X-ray | 2.25 Å | A/B=703-1047 |
| 5MY6 | X-ray | 2.25 Å | A=24-645 |
| 1QR1 | X-ray | 2.4 Å | C/F=654-662 |
| 3H3B | X-ray | 2.45 Å | A/B=23-214 |
| 2A91 | X-ray | 2.5 Å | A=22-530 |
| 4NND | X-ray | 2.5 Å | C/E/F/H=1109-1114 |
| 1N8Z | X-ray | 2.52 Å | C=23-629 |
| 4HRL | X-ray | 2.55 Å | C=24-219 |
| 8VQD | EM | 2.61 Å | A=23-652 |
Showing 20 of 63 experimental structures (best resolution first).
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