Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B(S1303D). Determined by X-ray diffraction at 2.4 Å resolution. Released 23 Dec 2020.
Explore 7KL1 in 3D Show helices and sheets RCSB PDB PDBe
7KL1 contains 30 α-helices and 30 β-strands across 4 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.
| 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 | 37-45 | 9 | 1 |
| α-helix | 51-66 | 16 | |
| β-strand | 72 | 1 | 2 |
| β-strand | 75-81 | 7 | 1 |
| β-strand | 84-90 | 7 | 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 |
| β-strand | 175 | 1 | 5 |
| α-helix | 177-179 | 3 | |
| α-helix | 182-186 | 5 | |
| β-strand | 190 | 1 | 4 |
| α-helix | 193-208 | 16 | |
| α-helix | 218-226 | 9 | |
| α-helix | 242-251 | 10 | |
| α-helix | 260-261 | 2 | |
| α-helix | 262-267 | 6 | |
| α-helix | 269-272 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-12 | 5 | |
| β-strand | 13-21 | 9 | 6 |
| β-strand | 25-32 | 8 | 6 |
| α-helix | 33-35 | 3 | |
| β-strand | 37-45 | 9 | 6 |
| α-helix | 51-66 | 16 | |
| β-strand | 72 | 1 | 7 |
| β-strand | 75-81 | 7 | 6 |
| β-strand | 84-90 | 7 | 6 |
| β-strand | 96 | 1 | 7 |
| α-helix | 97-104 | 8 | |
| α-helix | 109-128 | 20 | |
| β-strand | 131-132 | 2 | 8 |
| α-helix | 138-140 | 3 | |
| β-strand | 141-143 | 3 | 7 |
| β-strand | 152-154 | 3 | 7 |
| β-strand | 161-162 | 2 | 8 |
| β-strand | 169 | 1 | 9 |
| β-strand | 174-175 | 2 | 10 |
| α-helix | 177-179 | 3 | |
| α-helix | 182-185 | 4 | |
| β-strand | 190 | 1 | 9 |
| α-helix | 193-208 | 16 | |
| α-helix | 218-227 | 10 | |
| α-helix | 242-251 | 10 | |
| α-helix | 260-261 | 2 | |
| α-helix | 262-267 | 6 | |
| α-helix | 269-272 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1304 | 1 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1296-1298 | 3 | |
| β-strand | 1304-1305 | 2 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Calcium/calmodulin-dependent protein kinase type II subunit alpha | A, B | protein | 268 | Homo sapiens | Q9UQM7 (AlphaFold model) |
| Glutamate receptor ionotropic, NMDA 2B | C, D | protein | 22 | Homo sapiens | Q13224 (AlphaFold model) |
>7KL1_1 Calcium/calmodulin-dependent protein kinase type II subunit alpha (chains A, B) TRFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRL LKHPNIVRLHDSISEEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHC HQMGVVHRNLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVLR KDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYKQIKAGAYDFPSPEWDTVTPEAKD LINKMLTINPSKRITAAEALKHPWISHR
>7KL1_2 Glutamate receptor ionotropic, NMDA 2B (chains C, D) KAQKKNRNKLRRQHDYDTFVDL
Water and common crystallization additives (EDO) are not listed.
CaMKII binds both substrates and activators at the active site. Ozden, C., Sloutsky, R., Mitsugi, T. et al. Cell Rep (2022) 40:111064-111064. DOI 10.1016/j.celrep.2022.111064 · 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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