5IG3: Human CaMKII-alpha hub
Crystal structure of the human CaMKII-alpha hub. Determined by X-ray diffraction at 2.75 Å resolution. Released 23 Mar 2016.
- Method
- X-ray diffraction
- Resolution
- 2.75 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 6,312
- Mol. weight
- 105.12 kDa
- Released
- 23 Mar 2016
Explore 5IG3 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5IG3 contains 29 α-helices and 38 β-strands across 6 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: 7 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 330-332 | 3 | 1 |
| α-helix | 336-339 | 4 | |
| α-helix | 344-362 | 19 | |
| α-helix | 366-371 | 6 | |
| β-strand | 373-380 | 8 | 1 |
| α-helix | 382-384 | 3 | |
| β-strand | 389-390 | 2 | 1 |
| α-helix | 393-397 | 5 | |
| α-helix | 398-403 | 6 | |
| α-helix | 404-405 | 2 | |
| β-strand | 411-421 | 11 | 1 |
| β-strand | 426-438 | 13 | 1 |
| β-strand | 444-458 | 15 | 1 |
| β-strand | 461-470 | 10 | 1 |
Chain B: 5 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 345-363 | 19 | |
| α-helix | 366-371 | 6 | |
| β-strand | 373-380 | 8 | 2 |
| α-helix | 382-384 | 3 | |
| β-strand | 388-390 | 3 | 2 |
| α-helix | 393-397 | 5 | |
| α-helix | 398-402 | 5 | |
| β-strand | 411-421 | 11 | 2 |
| β-strand | 426-438 | 13 | 2 |
| β-strand | 444-458 | 15 | 2 |
| β-strand | 461-471 | 11 | 2 |
Chain C: 4 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 332-333 | 2 | 3 |
| α-helix | 344-362 | 19 | |
| α-helix | 366-371 | 6 | |
| β-strand | 373-380 | 8 | 3 |
| α-helix | 382-384 | 3 | |
| β-strand | 388-390 | 3 | 3 |
| α-helix | 393-400 | 8 | |
| β-strand | 411-421 | 11 | 3 |
| β-strand | 426-438 | 13 | 3 |
| β-strand | 444-457 | 14 | 3 |
| β-strand | 462-470 | 9 | 3 |
Chain D: 5 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 347-362 | 16 | |
| α-helix | 366-371 | 6 | |
| β-strand | 373-380 | 8 | 4 |
| α-helix | 382-384 | 3 | |
| α-helix | 387 | 1 | |
| β-strand | 388-390 | 3 | 4 |
| α-helix | 393-401 | 9 | |
| β-strand | 411-421 | 11 | 4 |
| β-strand | 426-438 | 13 | 4 |
| β-strand | 444-457 | 14 | 4 |
| β-strand | 462-471 | 10 | 4 |
Chain E: 4 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 347-362 | 16 | |
| α-helix | 366-371 | 6 | |
| β-strand | 373-380 | 8 | 5 |
| α-helix | 382-384 | 3 | |
| β-strand | 389-390 | 2 | 5 |
| α-helix | 393-399 | 7 | |
| β-strand | 411-421 | 11 | 5 |
| β-strand | 426-438 | 13 | 5 |
| β-strand | 444-457 | 14 | 5 |
| β-strand | 462-470 | 9 | 5 |
Chain F: 4 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 347-362 | 16 | |
| α-helix | 366-372 | 7 | |
| β-strand | 373-380 | 8 | 6 |
| α-helix | 382-384 | 3 | |
| β-strand | 389-390 | 2 | 6 |
| α-helix | 393-396 | 4 | |
| β-strand | 411-421 | 11 | 6 |
| β-strand | 426-439 | 14 | 6 |
| β-strand | 443-457 | 15 | 6 |
| β-strand | 462-471 | 10 | 6 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Calcium/calmodulin-dependent protein kinase type II subunit alpha | A, B, C, D, E, F | protein | 153 | Homo sapiens | Q9UQM7 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>5IG3_1 Calcium/calmodulin-dependent protein kinase type II subunit alpha (chains A, B, C, D, E, F)
GSSHHHHHHSSGLEVLFQGPHMVRKQEIIKVTEQLIEAISNGDFESYTKMCDPGMTAFEP
EALGNLVEGLDFHRFYFENLWSRNSKPVHTTILNPHIHLMGDESACIAYIRITQYLDAGG
IPRTAQSEETRVWHRRDGKWQIVHFHRSGAPSV
Primary citation
Molecular mechanism of activation-triggered subunit exchange in Ca(2+)/calmodulin-dependent protein kinase II. Bhattacharyya, M., Stratton, M.M., Going, C.C. et al. Elife (2016) 5. DOI 10.7554/eLife.13405 · PubMed
Other PDB entries of the same protein (UniProt Q9UQM7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6X5G 1.85 Å, Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and LRRC7 inhibitory…
- 7UJR 1.95 Å, Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B
- 6OF8 2.1 Å, Structure of Thr354Asn, Glu355Gln, Thr412Asn, Ile414Met, Ile464His, and Phe467Met mutant…
- 7UJT 2.1 Å, Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B(S1303D) in…
- 9EOY 2.1 Å, Structure of Thr354Asn, Glu355Gln, Thr412Asn, Ile414Met, Ile464His, and Phe467Met mutant…
- 6X5Q 2.14 Å, Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluA1
- 7REC 2.2 Å, Structure of Thr354Asn, Glu355Gln, Thr412Asn, Ile414Met, Ile464His, and Phe467Met mutant…
- 7UJQ 2.25 Å, Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B
- 2VZ6 2.3 Å, Structure of human calcium calmodulin dependent protein kinase type II alpha (CAMK2A) in…
- 7KL0 2.4 Å, Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B(S1303D)
- 7KL1 2.4 Å, Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B(S1303D)
- 6VZK 2.55 Å, Crystal structure of human CaMKII-alpha (CAMK2A)kinase domain
Browse structure collections
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