Full-length human CaMKII. Determined by X-ray diffraction at 3.55 Å resolution. Released 31 Aug 2011.
Explore 3SOA in 3D Show helices and sheets RCSB PDB PDBe
3SOA contains 18 α-helices and 23 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 | 8-12 | 5 | |
| β-strand | 13-21 | 9 | 1 |
| β-strand | 26-32 | 7 | 1 |
| β-strand | 37-45 | 9 | 1 |
| α-helix | 50-66 | 17 | |
| β-strand | 69 | 1 | 2 |
| β-strand | 72 | 1 | 2 |
| β-strand | 75-80 | 6 | 1 |
| β-strand | 84-89 | 6 | 1 |
| β-strand | 93 | 1 | 3 |
| β-strand | 96 | 1 | 2 |
| α-helix | 97-103 | 7 | |
| α-helix | 109-128 | 20 | |
| β-strand | 132 | 1 | 4 |
| β-strand | 141-143 | 3 | 2 |
| β-strand | 145 | 1 | 3 |
| α-helix | 150-151 | 2 | |
| β-strand | 152-154 | 3 | 2 |
| β-strand | 161 | 1 | 4 |
| β-strand | 169 | 1 | 5 |
| α-helix | 177-179 | 3 | |
| α-helix | 182-185 | 4 | |
| β-strand | 190 | 1 | 5 |
| α-helix | 193-208 | 16 | |
| α-helix | 218-227 | 10 | |
| α-helix | 242-251 | 10 | |
| α-helix | 262-267 | 6 | |
| α-helix | 272-277 | 6 | |
| α-helix | 284-300 | 17 | |
| β-strand | 306-307 | 2 | 6 |
| α-helix | 315-333 | 19 | |
| α-helix | 337-342 | 6 | |
| β-strand | 343-350 | 8 | 6 |
| α-helix | 352-354 | 3 | |
| β-strand | 358-360 | 3 | 6 |
| α-helix | 361-364 | 4 | |
| α-helix | 366-371 | 6 | |
| β-strand | 381-392 | 12 | 6 |
| β-strand | 396-408 | 13 | 6 |
| β-strand | 414-428 | 15 | 6 |
| β-strand | 431-441 | 11 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Calcium/calmodulin-dependent protein kinase type II subunit alpha with a beta 7 linker | A | protein | 444 | Homo sapiens | Q9UQM7 (AlphaFold model) |
>3SOA_1 Calcium/calmodulin-dependent protein kinase type II subunit alpha with a beta 7 linker (chains A) MATITCTRFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAMIINTKKLSARDHQKLERE ARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQIL EAVLHCHQMGVVHRNLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAWFGFAGTPGYL SPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTV TPEAKDLINKMLTINPSKRITAAEALKHPWISHRSTVASCMHRQETVDCLKKFNARRKLK GAILTVMLATRNFSVRKQEIIKVTEQLIEAISNGDFESYTKMCDPGMTAFEPEALGNLVE GLDFHRFYFENLWSRNSKPVHTTILNPHIHLMGDESACIAYIRITQYLDAGGIPRTAQSE ETRVWHRRDGKWQIVHFHRSGAPS
| ID | Name | Formula | Copies |
|---|---|---|---|
| DB8 | 4-[(2,4-dichloro-5-methoxyphenyl)amino]-6-methoxy-7-[3-(4-methylpiperazin-1-yl)… | C26 H29 Cl2 N5 O3 | 1 |
A Mechanism for Tunable Autoinhibition in the Structure of a Human Ca(2+)/Calmodulin- Dependent Kinase II Holoenzyme. Chao, L.H., Stratton, M.M., Lee, I.H. et al. Cell (2011) 146:732-745. DOI 10.1016/j.cell.2011.07.038 · PubMed
Other PDB entries of the same protein (UniProt Q9UQM7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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