Crystal structure of human CaMKII-alpha (CAMK2A)kinase domain. Determined by X-ray diffraction at 2.55 Å resolution. Released 22 Apr 2020.
Explore 6VZK in 3D Show helices and sheets RCSB PDB PDBe
6VZK contains 15 α-helices and 14 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 | 25-32 | 8 | 1 |
| α-helix | 33-35 | 3 | |
| β-strand | 37-44 | 8 | 1 |
| α-helix | 54-66 | 13 | |
| β-strand | 69 | 1 | 2 |
| β-strand | 72 | 1 | 2 |
| β-strand | 75-81 | 7 | 1 |
| β-strand | 84-89 | 6 | 1 |
| β-strand | 96 | 1 | 2 |
| α-helix | 97-104 | 8 | |
| α-helix | 109-128 | 20 | |
| β-strand | 131-132 | 2 | 3 |
| α-helix | 138-140 | 3 | |
| β-strand | 141-143 | 3 | 2 |
| α-helix | 150-151 | 2 | |
| β-strand | 152-154 | 3 | 2 |
| β-strand | 161-162 | 2 | 3 |
| β-strand | 169 | 1 | 4 |
| α-helix | 177-179 | 3 | |
| α-helix | 182-185 | 4 | |
| β-strand | 190 | 1 | 4 |
| α-helix | 193-208 | 16 | |
| α-helix | 218-227 | 10 | |
| α-helix | 242-251 | 10 | |
| α-helix | 260-261 | 2 | |
| α-helix | 262-266 | 5 | |
| α-helix | 269-272 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Calcium/calmodulin-dependent protein kinase type II subunit alpha | A | protein | 268 | Homo sapiens | Q9UQM7 (AlphaFold model) |
>6VZK_1 Calcium/calmodulin-dependent protein kinase type II subunit alpha (chains A) TRFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRL LKHPNIVRLHDSISEEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHC HQMGVVHRNLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVLR KDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYKQIKAGAYDFPSPEWDTVTPEAKD LINKMLTINPSKRITAAEALKHPWISHR
| ID | Name | Formula | Copies |
|---|---|---|---|
| HC4 | 4'-hydroxycinnamic acid | C9 H8 O3 | 1 |
Characterization of CaMKII alpha holoenzyme stability. Torres-Ocampo, A.P., Ozden, C., Hommer, A. et al. Protein Sci (2020) 29:1524-1534. DOI 10.1002/pro.3869 · 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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