High resolution crystal structure of the Pleckstrin Homology Domain Of Protein Kinase B/Akt Bound To Ins(1,3,4,5)-Tetrakisphophate. Determined by X-ray diffraction at 0.98 Å resolution. Released 16 Sept 2004.
Explore 1UNQ in 3D Show helices and sheets RCSB PDB PDBe
1UNQ contains 3 α-helices and 7 β-strands across 1 chain. 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 | 2-4 | 3 | |
| β-strand | 6-15 | 10 | 1 |
| β-strand | 22-30 | 9 | 1 |
| β-strand | 34-38 | 5 | 1 |
| α-helix | 45-48 | 4 | |
| β-strand | 53-56 | 4 | 1 |
| β-strand | 61-65 | 5 | 1 |
| β-strand | 72-79 | 8 | 1 |
| β-strand | 82-89 | 8 | 1 |
| α-helix | 93-115 | 23 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Rac-alpha serine/threonine kinase | A | protein | 125 | HOMO SAPIENS | P31749 (AlphaFold model) |
>1UNQ_1 RAC-ALPHA SERINE/THREONINE KINASE (chains A) XSMSDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQREAPLNNFSVA QCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKKQEEEEM DFRSG
| ID | Name | Formula | Copies |
|---|---|---|---|
| 4IP | Inositol-(1,3,4,5)-tetrakisphosphate | C6 H16 O18 P4 | 1 |
Binding of phosphatidylinositol 3,4,5-trisphosphate to the pleckstrin homology domain of protein kinase B induces a conformational change. Milburn, C.C., Deak, M., Kelly, S.M. et al. Biochem J (2003) 375:531-538. DOI 10.1042/BJ20031229 · PubMed
Other PDB entries of the same protein (UniProt P31749 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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