Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and Tiam1 in complex with ATP. Determined by X-ray diffraction at 3.1 Å resolution. Released 6 Apr 2022.
Explore 7UIR in 3D Show helices and sheets RCSB PDB PDBe
7UIR contains 29 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 |
|---|---|---|---|
| β-strand | 13-21 | 9 | 1 |
| β-strand | 25-32 | 8 | 1 |
| β-strand | 37-44 | 8 | 1 |
| α-helix | 46-48 | 3 | |
| α-helix | 51-64 | 14 | |
| β-strand | 69 | 1 | 2 |
| β-strand | 72 | 1 | 2 |
| β-strand | 75-80 | 6 | 1 |
| β-strand | 85-89 | 5 | 1 |
| α-helix | 90-91 | 2 | |
| 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 |
| 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 | 218-226 | 9 | |
| α-helix | 242-251 | 10 | |
| α-helix | 260-261 | 2 | |
| α-helix | 262-266 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 13-21 | 9 | 5 |
| β-strand | 25-32 | 8 | 5 |
| β-strand | 37-44 | 8 | 5 |
| α-helix | 52-64 | 13 | |
| β-strand | 69 | 1 | 6 |
| β-strand | 72 | 1 | 6 |
| β-strand | 75-80 | 6 | 5 |
| β-strand | 85-89 | 5 | 5 |
| α-helix | 90-91 | 2 | |
| β-strand | 96 | 1 | 6 |
| α-helix | 97-104 | 8 | |
| α-helix | 109-128 | 20 | |
| β-strand | 131-132 | 2 | 7 |
| α-helix | 138-140 | 3 | |
| β-strand | 141-143 | 3 | 6 |
| β-strand | 152-154 | 3 | 6 |
| β-strand | 161-162 | 2 | 7 |
| β-strand | 169 | 1 | 8 |
| α-helix | 177-179 | 3 | |
| α-helix | 182-185 | 4 | |
| β-strand | 190 | 1 | 8 |
| α-helix | 193-208 | 16 | |
| β-strand | 217 | 1 | 9 |
| α-helix | 218-226 | 9 | |
| α-helix | 242-251 | 10 | |
| α-helix | 260-261 | 2 | |
| α-helix | 262-266 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1542 | 1 | 9 |
| α-helix | 1546-1549 | 4 | |
| α-helix | 1550-1552 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1546-1549 | 4 | |
| α-helix | 1550-1552 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Calcium/calmodulin-dependent protein kinase type II subunit alpha | A, B | protein | 268 | Homo sapiens | Q9UQM7 (AlphaFold model) |
| T-lymphoma invasion and metastasis-inducing protein 1 | C, D | protein | 19 | Mus musculus | Q60610 (AlphaFold model) |
>7UIR_1 Calcium/calmodulin-dependent protein kinase type II subunit alpha (chains A, B) TRFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRL LKHPNIVRLHDSISEEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHC HQMGVVHRNLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVLR KDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYKQIKAGAYDFPSPEWDTVTPEAKD LINKMLTINPSKRITAAEALKHPWISHR
>7UIR_2 T-lymphoma invasion and metastasis-inducing protein 1 (chains C, D) RTLDSHASRMTQLKKQAAL
Water and common crystallization additives (EPE) 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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