Dual specificity mitogen-activated protein kinase kinase 7 (MAP2K7) is a 419-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O14733.
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The mean pLDDT of this model is 77.3 (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 | 44% |
| 70 to 90 | Confident: backbone generally right | 26% |
| 50 to 70 | Low: treat with caution | 11% |
| Below 50 | Very low: often disordered regions | 19% |
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. Essential component of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. With MAP2K4/MKK4, is the one of the only known kinase to directly activate the stress-activated protein kinase/c-Jun N-terminal kinases MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3. MAP2K4/MKK4 and MAP2K7/MKK7 both activate the JNKs by phosphorylation, but they differ in their preference for the phosphorylation site in the Thr-Pro-Tyr motif. MAP2K4/MKK4 shows preference for phosphorylation of the Tyr residue and MAP2K7/MKK7 for the Thr residue. The monophosphorylation of…
Interacts with isoform 1 of VRK2. Interacts (via its D domain) with its substrates MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3 (By similarity). Interacts (via its DVD domain) with MAP3Ks activators like MAP3K5/ASK1 and MAP3K1/MEKK1 (By similarity). Interacts with MAPK8IP1/JIP1, MAPK8IP2/JIP2 and MAPK8IP3/JIP3 scaffold proteins. Interacts with RASSF7, the interaction promotes phosphorylation. Found in…
Nucleus, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5Y90 | X-ray | 1.3 Å | A=103-419 |
| 6YZ4 | X-ray | 1.7 Å | A=100-405 |
| 6YFZ | X-ray | 1.9 Å | A=100-405 |
| 7OVI | X-ray | 1.95 Å | A=101-408 |
| 6YG0 | X-ray | 2.0 Å | A=100-405 |
| 6YG2 | X-ray | 2.0 Å | A=100-405 |
| 6YG3 | X-ray | 2.05 Å | A=100-405 |
| 7OVK | X-ray | 2.05 Å | A=101-408 |
| 7CBX | X-ray | 2.06 Å | A=103-419 |
| 5B2L | X-ray | 2.1 Å | A=103-419 |
| 6IB2 | X-ray | 2.1 Å | A=101-408 |
| 6QG7 | X-ray | 2.1 Å | A=101-408 |
| 6YG6 | X-ray | 2.15 Å | A/B=100-405 |
| 6QFL | X-ray | 2.2 Å | A=101-408 |
| 6YG7 | X-ray | 2.2 Å | A/B=100-405 |
| 6YG1 | X-ray | 2.22 Å | A/B/C=60-405 |
| 9HZ0 | X-ray | 2.25 Å | A=101-408 |
| 5Z1D | X-ray | 2.28 Å | A=103-419 |
| 5Z1E | X-ray | 2.3 Å | A=103-419 |
| 6QFR | X-ray | 2.3 Å | A=101-408 |
Showing 20 of 37 experimental structures (best resolution first).
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