Target of rapamycin complex 2 subunit MAPKAP1 (MAPKAP1) is a 522-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9BPZ7.
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The mean pLDDT of this model is 69.2 (low 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 | 9% |
| 70 to 90 | Confident: backbone generally right | 47% |
| 50 to 70 | Low: treat with caution | 28% |
| Below 50 | Very low: often disordered regions | 16% |
What pLDDT means and how to read it
Component of the mechanistic target of rapamycin complex 2 (mTORC2), which transduces signals from growth factors to pathways involved in proliferation, cytoskeletal organization, lipogenesis and anabolic output (PubMed:15467718, PubMed:16919458, PubMed:16962653, PubMed:17043309, PubMed:21806543, PubMed:28264193, PubMed:28968999, PubMed:30837283, PubMed:35926713). In response to growth factors, mTORC2 phosphorylates and activates AGC protein kinase family members, including AKT (AKT1, AKT2 and AKT3), PKC (PRKCA, PRKCB and PRKCE) and SGK1 (PubMed:16919458, PubMed:16962653, PubMed:21806543, PubMed:28264193, PubMed:28968999, PubMed:30837283, PubMed:35926713). In contrast to mTORC1, mTORC2 is…
Component of the mechanistic target of rapamycin complex 2 (mTORC2), consisting in two heterotretramers composed of MTOR, MLST8, RICTOR and MAPKAP1/SIN1 (PubMed:16919458, PubMed:16962653, PubMed:28264193, PubMed:29424687, PubMed:29567957, PubMed:33378666, PubMed:34519268, PubMed:35926713). The mTORC2 core complex associates with PRR5/PROTOR1 and/or PRR5L/PROTOR2 (PubMed:29424687). Contrary to…
Cell membrane, Endoplasmic reticulum membrane, Early endosome membrane, Late endosome membrane, Lysosome membrane, Golgi apparatus membrane, Mitochondrion outer membrane, Cytoplasm, perinuclear region, Nucleus, Cytoplasm, cytosol, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7VV9 | X-ray | 1.6 Å | C=275-360 |
| 7VV8 | X-ray | 1.7 Å | C=274-360 |
| 7VVB | X-ray | 1.7 Å | B=1-522 |
| 7VVG | X-ray | 1.7 Å | C=274-360 |
| 3VOQ | X-ray | 2.0 Å | A/B=372-493 |
| 7LC1 | X-ray | 2.35 Å | B/D=275-510 |
| 9T94 | EM | 2.6 Å | G=2-522 |
| 9ZBK | EM | 2.6 Å | D=1-266 |
| 7LC2 | X-ray | 2.7 Å | D/E=275-361 |
| 9T93 | EM | 2.86 Å | G=2-522 |
| 6ZWO | EM | 3.0 Å | H=2-522 |
| 9T7J | EM | 3.0 Å | G/H=2-522 |
| 9TDT | EM | 3.0 Å | G=2-522 |
| 9T92 | EM | 3.1 Å | G/H=2-522 |
| 6ZWM | EM | 3.2 Å | G/H=1-522 |
| 7PE8 | EM | 3.2 Å | G=1-522 |
| 9ZBJ | EM | 3.2 Å | D=1-148 |
| 7TZO | EM | 3.28 Å | G/H=1-522 |
| 9TDS | EM | 3.3 Å | G/H=2-522 |
| 7PE7 | EM | 3.41 Å | G/H=1-522 |
Showing 20 of 23 experimental structures (best resolution first).
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