Crystal structure of the PKA-Protein A fusion protein (end-to-end fusion). Determined by X-ray diffraction at 3.25 Å resolution. Released 5 Jul 2017.
Explore 5XBY in 3D Show helices and sheets RCSB PDB PDBe
5XBY contains 18 α-helices and 0 β-strands across 4 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 | 9-23 | 15 | |
| α-helix | 28-41 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-6 | 2 | |
| α-helix | 9-23 | 15 | |
| α-helix | 28-55 | 28 | |
| α-helix | 62-74 | 13 | |
| α-helix | 76-78 | 3 | |
| α-helix | 79-92 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-23 | 15 | |
| α-helix | 28-51 | 24 | |
| α-helix | 54-56 | 3 | |
| α-helix | 62-74 | 13 | |
| α-helix | 80-92 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-23 | 15 | |
| α-helix | 28-56 | 29 | |
| α-helix | 62-74 | 13 | |
| α-helix | 76-78 | 3 | |
| α-helix | 79-92 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| cAMP-dependent protein kinase type II-alpha regulatory subunit,Immunoglobulin G-binding protein A | A, B, C, D | protein | 97 | Homo sapiens, Staphylococcus aureus | P13861 (AlphaFold model), P38507 (AlphaFold model) |
>5XBY_1 cAMP-dependent protein kinase type II-alpha regulatory subunit,Immunoglobulin G-binding protein A (chains A, B, C, D) GSPWQIPPGLTELLQGYTVEVLRQQPPDLVEFAVEYFTRLREARNKEQQNAFYEILHLPN LNEEQRNAFIQSLKDDPSQSANLLAEAKKLNDAQAPK
Construction of novel repeat proteins with rigid and predictable structures using a shared helix method. Youn, S.J., Kwon, N.Y., Lee, J.H. et al. Sci Rep (2017) 7:2595-2595. DOI 10.1038/s41598-017-02803-z · PubMed
Other PDB entries of the same protein (UniProt P13861 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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