5H77: PKA-protein A fusion protein
Crystal structure of the PKA-protein A fusion protein. Determined by X-ray diffraction at 3.2 Å resolution. Released 28 Jun 2017.
- Method
- X-ray diffraction
- Resolution
- 3.2 Å
- Organisms
- Homo sapiens, Staphylococcus aureus
- Chains
- 12
- Atoms
- 8,143
- Mol. weight
- 123.77 kDa
- Released
- 28 Jun 2017
Explore 5H77 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5H77 contains 52 α-helices and 0 β-strands across 12 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.
Chain A: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-21 | 15 | |
| α-helix | 26-47 | 22 | |
| α-helix | 54-65 | 12 | |
| α-helix | 71-82 | 12 | |
Chain B: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-4 | 2 | |
| α-helix | 7-21 | 15 | |
| α-helix | 26-48 | 23 | |
| α-helix | 54-66 | 13 | |
| α-helix | 71-85 | 15 | |
Chain C: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-21 | 15 | |
| α-helix | 26-47 | 22 | |
| α-helix | 54-66 | 13 | |
| α-helix | 71-83 | 13 | |
Chain D: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-4 | 2 | |
| α-helix | 7-21 | 15 | |
| α-helix | 26-46 | 21 | |
| α-helix | 54-66 | 13 | |
| α-helix | 71-82 | 12 | |
Chain E: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-4 | 2 | |
| α-helix | 7-21 | 15 | |
| α-helix | 26-48 | 23 | |
| α-helix | 54-66 | 13 | |
| α-helix | 71-80 | 10 | |
Chain F: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-21 | 15 | |
| α-helix | 26-47 | 22 | |
| α-helix | 54-66 | 13 | |
| α-helix | 71-84 | 14 | |
Chains G and I: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-21 | 15 | |
| α-helix | 26-47 | 22 | |
| α-helix | 54-66 | 13 | |
| α-helix | 73-80 | 8 | |
Chain H: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-4 | 2 | |
| α-helix | 7-21 | 15 | |
| α-helix | 26-46 | 21 | |
| α-helix | 54-66 | 13 | |
| α-helix | 71-81 | 11 | |
3 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| cAMP-dependent protein kinase type II-alpha regulatory subunit,Immunoglobulin G-binding protein A | A, B, C, D, E, F, G, H, I, J, K, L | protein | 90 | Homo sapiens, Staphylococcus aureus | P13861 (AlphaFold model), P38507 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J, K, L), FASTA
>5H77_1 cAMP-dependent protein kinase type II-alpha regulatory subunit,Immunoglobulin G-binding protein A (chains A, B, C, D, E, F, G, H, I, J, K, L)
GSPWQIPPGLTELLQGYTVEVLRQQPPDLVEFAVEYFTRLRQQRAFYEILHLPNLNEEQR
NAFIQSLKDDPSQSANLLAEAKKLNDAQAP
Primary citation
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:
- 2IZX 1.3 Å, Molecular Basis of AKAP Specificity for PKA Regulatory Subunits
- 5H78 2.0 Å, Crystal structure of the PKA-DHR14 fusion protein
- 9NXN 2.1 Å, Crystal structure of CN:RII alpha
- 4ZP3 2.63 Å, AKAP18:PKA-RIIalpha structure reveals crucial anchor points for recognition of…
- 5XBY 3.25 Å, Crystal structure of the PKA-Protein A fusion protein (end-to-end fusion)
- 2KYG Structure of the AML1-ETO Nervy Domain - PKA(RIIa) complex and its contribution to…
- 8S8O Solution Structure of cAMP-dependent Protein Kinase RII-alpha Subunit Dimerization and…
Browse structure collections
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