Structure of the Bovine p85alpha BH domain, R262T mutant. Determined by X-ray diffraction at 2.7 Å resolution. Released 23 May 2018.
Explore 6D87 in 3D Show helices and sheets RCSB PDB PDBe
6D87 contains 25 α-helices and 0 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 115-117 | 3 | |
| α-helix | 118-121 | 4 | |
| α-helix | 130-143 | 14 | |
| α-helix | 158-164 | 7 | |
| α-helix | 174-176 | 3 | |
| α-helix | 179-192 | 14 | |
| α-helix | 200-207 | 8 | |
| α-helix | 216-227 | 12 | |
| α-helix | 234-251 | 18 | |
| α-helix | 254-257 | 4 | |
| α-helix | 261-273 | 13 | |
| α-helix | 283-295 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 115-117 | 3 | |
| α-helix | 118-121 | 4 | |
| α-helix | 130-143 | 14 | |
| α-helix | 158-166 | 9 | |
| α-helix | 174-176 | 3 | |
| α-helix | 179-192 | 14 | |
| α-helix | 200-208 | 9 | |
| α-helix | 216-227 | 12 | |
| α-helix | 234-251 | 18 | |
| α-helix | 254-257 | 4 | |
| α-helix | 261-269 | 9 | |
| α-helix | 270-274 | 5 | |
| α-helix | 284-295 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Phosphatidylinositol 3-kinase regulatory subunit alpha | A, B | protein | 193 | Bos taurus | P23727 (AlphaFold model) |
>6D87_1 Phosphatidylinositol 3-kinase regulatory subunit alpha (chains A, B) QQASTLPDLAEQFAPPDVAPPLLIKLVEAIEKKGLECSTLYRTQSSSNPAELRQLLDCDT ASLDLEMFDVHVLADAFKRYLLDLPNPVIPVAVSSELISLAPEVQSSEEYIQLLKKLIRS PSIPHQYWLTLQYLLKHFFKLSQTSSKNLLNATVLSELFSPLLFRFPAASSENTEHLIKI IEILISTEWNERQ
Patient-derived mutations within the N-terminal domains of p85 alpha impact PTEN or Rab5 binding and regulation. Mellor, P., Marshall, J.D.S., Ruan, X. et al. Sci Rep (2018) 8:7108-7108. DOI 10.1038/s41598-018-25487-5 · PubMed
Other PDB entries of the same protein (UniProt P23727 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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