9EOY: PDB entry 9EOY
Structure of Thr354Asn, Glu355Gln, Thr412Asn, Ile414Met, Ile464His, and Phe467Met mutant human CaMKII alpha hub bound to PIPA. Determined by X-ray diffraction at 2.1 Å resolution. Released 25 Sept 2024.
- Method
- X-ray diffraction
- Resolution
- 2.1 Å
- Organism
- Homo sapiens
- Chains
- 7
- Atoms
- 7,710
- Mol. weight
- 109.98 kDa
- Ligands
- A1H6K
- Released
- 25 Sept 2024
Explore 9EOY in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9EOY contains 35 α-helices and 42 β-strands across 7 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: 6 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 345-363 | 19 | |
| α-helix | 366-372 | 7 | |
| β-strand | 373-380 | 8 | 1 |
| α-helix | 382-384 | 3 | |
| β-strand | 389-390 | 2 | 1 |
| α-helix | 391-394 | 4 | |
| α-helix | 396-398 | 3 | |
| α-helix | 399-403 | 5 | |
| β-strand | 411-422 | 12 | 1 |
| β-strand | 426-438 | 13 | 1 |
| β-strand | 444-458 | 15 | 1 |
| β-strand | 461-471 | 11 | 1 |
Chain B: 5 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 343-363 | 21 | |
| α-helix | 366-372 | 7 | |
| β-strand | 373-380 | 8 | 2 |
| α-helix | 382-384 | 3 | |
| β-strand | 389-390 | 2 | 2 |
| α-helix | 391-398 | 8 | |
| α-helix | 399-403 | 5 | |
| β-strand | 410-421 | 12 | 2 |
| β-strand | 426-438 | 13 | 2 |
| β-strand | 444-458 | 15 | 2 |
| β-strand | 461-471 | 11 | 2 |
Chain C: 4 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 345-363 | 19 | |
| α-helix | 366-372 | 7 | |
| β-strand | 373-380 | 8 | 3 |
| α-helix | 382-384 | 3 | |
| β-strand | 389 | 1 | 3 |
| α-helix | 392-401 | 10 | |
| β-strand | 410-421 | 12 | 3 |
| β-strand | 426-438 | 13 | 3 |
| β-strand | 444-458 | 15 | 3 |
| β-strand | 461-471 | 11 | 3 |
Chain D: 5 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 345-363 | 19 | |
| α-helix | 366-372 | 7 | |
| β-strand | 373-380 | 8 | 4 |
| α-helix | 382-384 | 3 | |
| 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 |
| α-helix | 473-474 | 2 | |
Chain E: 5 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 343-363 | 21 | |
| α-helix | 366-372 | 7 | |
| β-strand | 373-380 | 8 | 5 |
| α-helix | 382-384 | 3 | |
| β-strand | 389-390 | 2 | 5 |
| α-helix | 391-398 | 8 | |
| α-helix | 399-403 | 5 | |
| β-strand | 411-421 | 11 | 5 |
| β-strand | 426-438 | 13 | 5 |
| β-strand | 444-458 | 15 | 5 |
| β-strand | 461-471 | 11 | 5 |
Chain F: 5 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 345-363 | 19 | |
| α-helix | 366-372 | 7 | |
| β-strand | 373-380 | 8 | 6 |
| α-helix | 382-384 | 3 | |
| β-strand | 389-390 | 2 | 6 |
| α-helix | 391-398 | 8 | |
| α-helix | 399-403 | 5 | |
| β-strand | 411-421 | 11 | 6 |
| β-strand | 426-438 | 13 | 6 |
| β-strand | 444-458 | 15 | 6 |
| β-strand | 461-471 | 11 | 6 |
Chain G: 5 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 345-363 | 19 | |
| α-helix | 366-372 | 7 | |
| β-strand | 373-380 | 8 | 7 |
| α-helix | 382-384 | 3 | |
| β-strand | 389-390 | 2 | 7 |
| α-helix | 393-398 | 6 | |
| α-helix | 399-403 | 5 | |
| β-strand | 411-422 | 12 | 7 |
| β-strand | 426-438 | 13 | 7 |
| β-strand | 444-458 | 15 | 7 |
| β-strand | 461-470 | 10 | 7 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Calcium/calmodulin-dependent protein kinase type II subunit alpha | A, B, C, D, E, F, G | protein | 135 | Homo sapiens | Q9UQM7 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G), FASTA
>9EOY_1 Calcium/calmodulin-dependent protein kinase type II subunit alpha (chains A, B, C, D, E, F, G)
GPHMVRKQEIIKVNQQLIEAISNGDFESYTKMCDPGMTAFEPEALGNLVEGLDFHRFYFE
NLWSRNSKPVHNTMLNPHIHLMGDESACIAYIRITQYLDAGGIPRTAQSEETRVWHRRDG
KWQHVHMHRSGAPSV
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| A1H6K | 2-[6-(4-chlorophenyl)imidazo[1,2-b]pyridazin-2-yl]ethanoic acid | C14 H10 Cl N3 O2 | 2 |
Water and common crystallization additives (PG4, ACT) are not listed.
Primary citation
Ligand-induced CaMKII alpha hub Trp403 flip, hub domain stacking, and modulation of kinase activity. Narayanan, D., Larsen, A.S.G., Gauger, S.J. et al. Protein Sci (2024) 33:e5152-e5152. DOI 10.1002/pro.5152 · 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…
- 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
- 7KL2 2.56 Å, Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B(S1303D)
Browse structure collections
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