Cryo-EM structure of the complex CDK16:CCNY:14-3-3. Determined by electron microscopy at 3.3 Å resolution. Released 25 Mar 2026.
Explore 9R2I in 3D Show helices and sheets RCSB PDB PDBe
9R2I contains 63 α-helices and 18 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 | 6-16 | 11 | |
| α-helix | 20-32 | 13 | |
| α-helix | 39-73 | 35 | |
| α-helix | 76-103 | 28 | |
| α-helix | 104-108 | 5 | |
| α-helix | 117-137 | 21 | |
| α-helix | 141-161 | 21 | |
| α-helix | 170-181 | 12 | |
| α-helix | 182-186 | 5 | |
| α-helix | 190-206 | 17 | |
| α-helix | 213-215 | 3 | |
| α-helix | 216-233 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-17 | 14 | |
| α-helix | 20-32 | 13 | |
| α-helix | 39-73 | 35 | |
| α-helix | 76-103 | 28 | |
| α-helix | 104-109 | 6 | |
| α-helix | 110-111 | 2 | |
| α-helix | 117-135 | 19 | |
| α-helix | 141-164 | 24 | |
| α-helix | 170-181 | 12 | |
| α-helix | 182-186 | 5 | |
| α-helix | 190-206 | 17 | |
| α-helix | 218-234 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 111-118 | 8 | |
| α-helix | 131-135 | 5 | |
| α-helix | 147-157 | 11 | |
| α-helix | 162-164 | 3 | |
| β-strand | 165-172 | 8 | 1 |
| β-strand | 177-184 | 8 | 1 |
| β-strand | 190-196 | 7 | 1 |
| β-strand | 199 | 1 | 2 |
| β-strand | 203 | 1 | 2 |
| α-helix | 206-215 | 10 | |
| β-strand | 223 | 1 | 3 |
| β-strand | 226-229 | 4 | 1 |
| β-strand | 238-241 | 4 | 1 |
| β-strand | 245-246 | 2 | 4 |
| α-helix | 247-253 | 7 | |
| α-helix | 260-279 | 20 | |
| β-strand | 282-283 | 2 | 5 |
| α-helix | 289-291 | 3 | |
| β-strand | 293-294 | 2 | 4 |
| β-strand | 300-301 | 2 | 4 |
| β-strand | 302 | 1 | 3 |
| β-strand | 309-310 | 2 | 5 |
| α-helix | 318-320 | 3 | |
| α-helix | 330-333 | 4 | |
| α-helix | 342-357 | 16 | |
| α-helix | 367-378 | 12 | |
| α-helix | 393-398 | 6 | |
| α-helix | 408-411 | 4 | |
| α-helix | 417-426 | 10 | |
| α-helix | 431-433 | 3 | |
| α-helix | 435-436 | 2 | |
| α-helix | 437-440 | 4 | |
| α-helix | 444-446 | 3 | |
| α-helix | 452-455 | 4 | |
| α-helix | 462-464 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 41-43 | 3 | |
| α-helix | 44-48 | 5 | |
| α-helix | 55-57 | 3 | |
| α-helix | 68-74 | 7 | |
| β-strand | 105 | 1 | 6 |
| α-helix | 116-132 | 17 | |
| α-helix | 156-158 | 3 | |
| α-helix | 165-167 | 3 | |
| α-helix | 168-182 | 15 | |
| α-helix | 186-203 | 18 | |
| α-helix | 213-228 | 16 | |
| α-helix | 246-260 | 15 | |
| α-helix | 268-283 | 16 | |
| α-helix | 292 | 1 | |
| β-strand | 293 | 1 | 6 |
| α-helix | 294 | 1 | |
| β-strand | 295 | 1 | 7 |
| α-helix | 296-302 | 7 | |
| α-helix | 306-309 | 4 | |
| α-helix | 314-318 | 5 | |
| α-helix | 323-325 | 3 | |
| β-strand | 337 | 1 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 14-3-3 protein eta | A, B | protein | 248 | Homo sapiens | Q04917 (AlphaFold model) |
| Cyclin-dependent kinase 16 | C | protein | 395 | Homo sapiens | Q00536 (AlphaFold model) |
| Cyclin-Y | D | protein | 346 | Homo sapiens | Q8ND76 (AlphaFold model) |
>9R2I_1 14-3-3 protein eta (chains A, B) GHMGDREQLLQRARLAEQAERYDDMASAMKAVTELNEPLSNEDRNLLSVAYKNVVGARRS SWRVISSIEQKTMADGNEKKLEKVKAYREKIEKELETVCNDVLSLLDKFLIKNCNDFQYE SKVFYLKMKGDYYRYLAEVASGEKKNSVVEASEAAYKEAFEISKEQMQPTHPIRLGLALN FSVFYYEIQNAPEQACLLAKQAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQ DEEAGEGN
>9R2I_2 Cyclin-dependent kinase 16 (chains C) GPLGSRKISTEDINKRLSLPADIRLPEGYLEKLTLNSPIFDKPLSRRLRRVSLSEIGFGK LETYIKLDKLGEGTYATVYKGKSKLTDNLVALKEIRLEHEEGAPCTAIREVSLLKDLKHA NIVTLHDIIHTEKSLTLVFEYLDKDLKQYLDDCGNIINMHNVKLFLFQLLRGLAYCHRQK VLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTYSNEVVTLWYRPPDILLGSTDYST QIDMWGVGCIFYEMATGRPLFPGSTVEEQLHFIFRILGTPTEETWPGILSNEEFKTYNYP KYRAEALLSHAPRLDSDGADLLTKLLQFEGRNRISAEDAMKHPFFLSLGERIHKLPDTTS IFALKEIQLQKEASLRSSSMPDSGRPAFRVVDTEF
>9R2I_3 Cyclin-Y (chains D) GPLGSMGNTTSCCVSSSPKLRRNAHSRLESYRPDTDLSREDTGCNLQHISDRENIDDLNM EFNPSDHPRASTIFLSKSQTDVREKRKSLFINHHPPGQIARKRASCSTIFLDDSTVSQPN LKYTIKCVALAIYYHIKNRDPDGRMLLDIFDENLHPLSKSEVPPDYDKHNPEQKQIYRFV RTLFSAAQLTAECAIVTLVYLERLLTYAEIDICPANWKRIVLGAILLASKVWDDQAVWNV DYCQILKDITVEDMNELERQFLELLQFNINVPSSVYAKYYFDLRSLAEANNLSFPLEPLS RERAHKLEAISRLCEDKYKDLRRSARKRAASADNLTLPRWSPAIIS
| ID | Name | Formula | Copies |
|---|---|---|---|
| AGS | Phosphothiophosphoric acid-adenylate ester | C10 H16 N5 O12 P3 S | 1 |
| MG | Magnesium ion | Mg | 1 |
Structural basis of the cyclin Y/14-3-3 protein-mediated activation of CDK16. Kohoutova, K., Kosek, D., Brzezina, A. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-70778-5 · PubMed
Other PDB entries of the same protein (UniProt Q04917 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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