Dual specificity mitogen-activated protein kinase kinase 1 (MAP2K1) is a 393-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q02750.
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The mean pLDDT of this model is 83.3 (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 | 61% |
| 70 to 90 | Confident: backbone generally right | 20% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 12% |
What pLDDT means and how to read it
Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Binding of extracellular ligands such as growth factors, cytokines and hormones to their cell-surface receptors activates RAS and this initiates RAF1 activation. RAF1 then further activates the dual-specificity protein kinases MAP2K1/MEK1 and MAP2K2/MEK2. Both MAP2K1/MEK1 and MAP2K2/MEK2 function specifically in the MAPK/ERK cascade, and catalyze the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in the extracellular signal-regulated kinases MAPK3/ERK1 and MAPK1/ERK2, leading to their activation and further transduction of…
Found in a complex with at least BRAF, HRAS, MAP2K1, MAPK3/ERK1 and RGS14 (By similarity). Forms a heterodimer with MAP2K2/MEK2 (By similarity). Forms heterodimers with KSR2 which further dimerize to form tetramers (By similarity). Interacts with KSR1 or KSR2 and BRAF; the interaction with KSR1 or KSR2 mediates KSR1-BRAF or KSR2-BRAF dimerization (PubMed:10409742, PubMed:29433126). Interacts…
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body, Cytoplasm, Nucleus, Membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7B7R | X-ray | 1.7 Å | A/B=37-263, A/B=308-383 |
| 7B9L | X-ray | 1.7 Å | A/B=37-263, A/B=308-383 |
| 3EQC | X-ray | 1.8 Å | A=35-393 |
| 3EQI | X-ray | 1.9 Å | A=35-393 |
| 3EQH | X-ray | 2.0 Å | A=35-393 |
| 3VVH | X-ray | 2.0 Å | A/B/C=62-393 |
| 7B94 | X-ray | 2.0 Å | A/B=37-263, A/B=308-383 |
| 7F2X | X-ray | 2.01 Å | A=45-392 |
| 9AXX | X-ray | 2.07 Å | A/C=37-263, A/C=308-383 |
| 3EQD | X-ray | 2.1 Å | A=35-393 |
| 4AN3 | X-ray | 2.1 Å | A=61-392 |
| 7XLP | X-ray | 2.1 Å | A=37-383 |
| 7XNC | X-ray | 2.1 Å | A=37-383 |
| 3ZLY | X-ray | 2.11 Å | A=37-383 |
| 3ZLW | X-ray | 2.12 Å | A=37-383 |
| 7PQV | X-ray | 2.13 Å | A=39-382 |
| 3W8Q | X-ray | 2.2 Å | A=39-382 |
| 3ZLX | X-ray | 2.2 Å | A=37-383 |
| 4ANB | X-ray | 2.2 Å | A=61-392 |
| 3DV3 | X-ray | 2.3 Å | A=62-382 |
Showing 20 of 94 experimental structures (best resolution first).
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