Crystal structure of the kinase domain of CIPK24/SOS2. Determined by X-ray diffraction at 3.3 Å resolution. Released 15 Oct 2014.
Explore 4D28 in 3D Show helices and sheets RCSB PDB PDBe
4D28 contains 56 α-helices and 43 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 | 11-13 | 3 | 1 |
| β-strand | 24-30 | 7 | 1 |
| β-strand | 35-43 | 9 | 1 |
| α-helix | 44-48 | 5 | |
| α-helix | 53-65 | 13 | |
| β-strand | 71 | 1 | 2 |
| β-strand | 77-79 | 3 | 1 |
| β-strand | 83-88 | 6 | 1 |
| β-strand | 94-95 | 2 | 2 |
| α-helix | 97-103 | 7 | |
| α-helix | 106-107 | 2 | |
| α-helix | 108-127 | 20 | |
| β-strand | 140-142 | 3 | 2 |
| β-strand | 148-150 | 3 | 2 |
| α-helix | 178-182 | 5 | |
| α-helix | 188-205 | 18 | |
| α-helix | 215-224 | 10 | |
| α-helix | 235-244 | 10 | |
| α-helix | 253-254 | 2 | |
| α-helix | 255-260 | 6 | |
| α-helix | 262-265 | 4 | |
| α-helix | 281-286 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8 | 1 | 3 |
| β-strand | 11-13 | 3 | 3 |
| β-strand | 20 | 1 | 4 |
| β-strand | 23 | 1 | 4 |
| β-strand | 24-30 | 7 | 3 |
| β-strand | 36-43 | 8 | 3 |
| α-helix | 44-48 | 5 | |
| α-helix | 53-65 | 13 | |
| β-strand | 71 | 1 | 5 |
| β-strand | 74-79 | 6 | 3 |
| β-strand | 83-89 | 7 | 3 |
| β-strand | 95 | 1 | 5 |
| α-helix | 97-103 | 7 | |
| α-helix | 106-107 | 2 | |
| α-helix | 108-128 | 21 | |
| α-helix | 137-139 | 3 | |
| β-strand | 140-142 | 3 | 5 |
| β-strand | 148-150 | 3 | 5 |
| α-helix | 178-181 | 4 | |
| α-helix | 188-205 | 18 | |
| α-helix | 215-224 | 10 | |
| α-helix | 228-230 | 3 | |
| α-helix | 235-244 | 10 | |
| α-helix | 253-254 | 2 | |
| α-helix | 255-259 | 5 | |
| α-helix | 262-265 | 4 | |
| α-helix | 270-272 | 3 | |
| α-helix | 281-286 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8 | 1 | 6 |
| β-strand | 11 | 1 | 6 |
| β-strand | 12-13 | 2 | 7 |
| β-strand | 24-29 | 6 | 7 |
| β-strand | 36-43 | 8 | 7 |
| α-helix | 44-48 | 5 | |
| α-helix | 53-65 | 13 | |
| β-strand | 71 | 1 | 8 |
| β-strand | 74-79 | 6 | 7 |
| β-strand | 83-89 | 7 | 7 |
| β-strand | 95 | 1 | 8 |
| α-helix | 96-103 | 8 | |
| α-helix | 106-107 | 2 | |
| α-helix | 108-127 | 20 | |
| α-helix | 137-139 | 3 | |
| β-strand | 140-142 | 3 | 8 |
| β-strand | 148-150 | 3 | 8 |
| α-helix | 178-182 | 5 | |
| α-helix | 188-205 | 18 | |
| α-helix | 215-224 | 10 | |
| α-helix | 235-244 | 10 | |
| α-helix | 253-254 | 2 | |
| α-helix | 255-259 | 5 | |
| α-helix | 262-265 | 4 | |
| α-helix | 281-286 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-13 | 2 | 9 |
| β-strand | 24-26 | 3 | 10 |
| β-strand | 28-29 | 2 | 9 |
| β-strand | 30 | 1 | 11 |
| α-helix | 31-33 | 3 | |
| β-strand | 35 | 1 | 11 |
| β-strand | 39-43 | 5 | 10 |
| α-helix | 44-48 | 5 | |
| α-helix | 53-64 | 12 | |
| β-strand | 71 | 1 | 12 |
| β-strand | 74-79 | 6 | 10 |
| β-strand | 83-88 | 6 | 10 |
| α-helix | 96-103 | 8 | |
| α-helix | 108-127 | 20 | |
| β-strand | 140-142 | 3 | 12 |
| β-strand | 148-150 | 3 | 12 |
| α-helix | 178-182 | 5 | |
| α-helix | 188-205 | 18 | |
| α-helix | 215-224 | 10 | |
| α-helix | 235-244 | 10 | |
| α-helix | 253-254 | 2 | |
| α-helix | 255-259 | 5 | |
| α-helix | 262-265 | 4 | |
| α-helix | 281-286 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cbl-interacting serine/threonine-protein kinase 24 | A, B, C, D | protein | 446 | ARABIDOPSIS THALIANA | Q9LDI3 (AlphaFold model) |
>4D28_1 CBL-INTERACTING SERINE/THREONINE-PROTEIN KINASE 24 (chains A, B, C, D) MTKKMRRVGKYEVGRTIGEGTFAKVKFARNTDTGDNVAIKIMAKSTILKNRMVDQIKREI SIMKIVRHPNIVRLYEVLASKSKIYIVLEFVTGGELFDRIVHKGRLKEDESRKYFQQLVD AVAHCHSKGVYHRDLKPENLLLDTNGNLKVSDFGLSALPQEGVELLNDTCGTPNYVAPEV LSGQGYDGSAADIWSCGVILFVILAGYLPFSETDLPGLYRKINAAEFDCPPWFSAEVKFL IHRILDPNPKTRIQIQGIKKDPWFRKNYVPIRAREEEEVNLDDIRAVFDGIEGSYVAENV ERNDEGPLMMNAFEMITLSQGLNLSALFDRRQDFVKRQTRFVSRREPSEIIANIEAVANS MGFKSHTRNFKTRLEGLSSIKAGQLAVVIEIYEVAPSLFMVDVRKAAGETLEYHKFYKKL CSKLENIIWRATEGIPKSEILRTITF
Structural Basis of the Regulatory Mechanism of the Plant Cipk Family of Protein Kinases Controlling Ion Homeostasis and Abiotic Stress. Chaves-Sanjuan, A., Sanchez-Barrena, M.J., Gonzalez-Rubio, J.M. et al. Proc Natl Acad Sci U S A (2014) 111:E4532. DOI 10.1073/PNAS.1407610111 · PubMed
Other PDB entries of the same protein (UniProt Q9LDI3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 4D28 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.