Hepatocyte growth factor receptor (MET) is a 1390-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P08581.
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The mean pLDDT of this model is 79.3 (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 | 43% |
| 70 to 90 | Confident: backbone generally right | 36% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 14% |
What pLDDT means and how to read it
Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphorylation of MET on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1. Recruitment of these downstream effectors by MET leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC.…
Heterodimer made of an alpha chain (50 kDa) and a beta chain (145 kDa) which are disulfide linked. Binds PLXNB1. Interacts when phosphorylated with downstream effectors including STAT3, PIK3R1, SRC, PCLG1, GRB2 and GAB1. Interacts with SPSB1, SPSB2 and SPSB4 (By similarity). Interacts with INPP5D/SHIP1. When phosphorylated at Tyr-1356, interacts with INPPL1/SHIP2. Interacts with RANBP9 and…
Membrane, Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9T6K | X-ray | 1.13 Å | A=1052-1346 |
| 4R1V | X-ray | 1.2 Å | A=1055-1345 |
| 9T0D | X-ray | 1.2 Å | A=1052-1346 |
| 9SXJ | X-ray | 1.31 Å | A=1052-1346 |
| 3BUX | X-ray | 1.35 Å | A/C=997-1009 |
| 3F66 | X-ray | 1.4 Å | A/B=1052-1349 |
| 3ZCL | X-ray | 1.4 Å | A=1051-1348 |
| 9T08 | X-ray | 1.46 Å | A=1052-1346 |
| 3DKC | X-ray | 1.52 Å | A=1049-1360 |
| 9T0B | X-ray | 1.54 Å | A=1038-1346 |
| 9C1R | X-ray | 1.59 Å | A=1048-1348 |
| 3Q6U | X-ray | 1.6 Å | A=1048-1348 |
| 4MXC | X-ray | 1.63 Å | A=1038-1346 |
| 9T3Q | X-ray | 1.63 Å | A=1038-1346 |
| 5HTI | X-ray | 1.66 Å | A=1038-1346 |
| 6SDC | X-ray | 1.67 Å | A=1038-1346 |
| 9T2V | X-ray | 1.67 Å | A=1052-1346 |
| 7V3R | X-ray | 1.7 Å | A=1038-1346 |
| 5HNI | X-ray | 1.71 Å | X/Y=1049-1360 |
| 3Q6W | X-ray | 1.75 Å | A=1048-1348 |
Showing 20 of 129 experimental structures (best resolution first).
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