9R2N: Complex CCNY:14-3-3

Cryo-EM structure of the complex CCNY:14-3-3. Determined by electron microscopy at 3.83 Å resolution. Released 25 Mar 2026.

Method: Electron microscopy
Resolution: 3.83 Å
Organism: Homo sapiens
Chains: 3
Atoms: 5,837
Mol. weight: 96.82 kDa
Released: 25 Mar 2026

Explore 9R2N in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9R2N contains 42 α-helices and 6 β-strands across 3 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.

Chain A: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	4-17	14
α-helix	20-32	13
α-helix	39-73	35
α-helix	77-103	27
α-helix	104-109	6
α-helix	110-111	2
α-helix	117-137	21
α-helix	141-163	23
α-helix	170-182	13
α-helix	183-187	5
α-helix	190-206	17
α-helix	216-233	18

Chain B: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	4-16	13
α-helix	20-31	12
α-helix	39-73	35
α-helix	76-103	28
α-helix	104-109	6
α-helix	110-111	2
α-helix	117-137	21
α-helix	140-164	25
α-helix	170-181	12
α-helix	182-186	5
α-helix	190-206	17
α-helix	209-211	3
α-helix	218-234	17

Chain D: 17 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	105	1	1
α-helix	116-132	17
β-strand	139	1	2
α-helix	143-145	3
α-helix	156-158	3
α-helix	159-162	4
α-helix	165-167	3
α-helix	168-182	15
α-helix	186-203	18
β-strand	205	1	2
α-helix	209-211	3
α-helix	213-227	15
α-helix	246-260	15
α-helix	268-283	16
α-helix	289-290	2
α-helix	292	1
β-strand	293	1	1
α-helix	294	1
β-strand	295	1	3
α-helix	296-302	7
α-helix	306-309	4
α-helix	323-325	3
β-strand	337	1	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein eta	A, B	protein	248	Homo sapiens	Q04917 (AlphaFold model)
Cyclin-Y	D	protein	346	Homo sapiens	Q8ND76 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>9R2N_1 14-3-3 protein eta (chains A, B)
GHMGDREQLLQRARLAEQAERYDDMASAMKAVTELNEPLSNEDRNLLSVAYKNVVGARRS
SWRVISSIEQKTMADGNEKKLEKVKAYREKIEKELETVCNDVLSLLDKFLIKNCNDFQYE
SKVFYLKMKGDYYRYLAEVASGEKKNSVVEASEAAYKEAFEISKEQMQPTHPIRLGLALN
FSVFYYEIQNAPEQACLLAKQAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQ
DEEAGEGN

Sequence of entity 2 (D), FASTA

>9R2N_2 Cyclin-Y (chains D)
GPLGSMGNTTSCCVSSSPKLRRNAHSRLESYRPDTDLSREDTGCNLQHISDRENIDDLNM
EFNPSDHPRASTIFLSKSQTDVREKRKSLFINHHPPGQIARKRASCSTIFLDDSTVSQPN
LKYTIKCVALAIYYHIKNRDPDGRMLLDIFDENLHPLSKSEVPPDYDKHNPEQKQIYRFV
RTLFSAAQLTAECAIVTLVYLERLLTYAEIDICPANWKRIVLGAILLASKVWDDQAVWNV
DYCQILKDITVEDMNELERQFLELLQFNINVPSSVYAKYYFDLRSLAEANNLSFPLEPLS
RERAHKLEAISRLCEDKYKDLRRSARKRAASADNLTLPRWSPAIIS

Primary citation

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:

2C63 2.15 Å, 14-3-3 Protein Eta (Human) Complexed to Peptide
7NMZ 2.3 Å, Structure of 14-3-3 eta in complex with Nedd4-2(335-455) containing two 14-3-3 binding…
2C74 2.7 Å, 14-3-3 Protein Eta (Human) Complexed to Peptide
9R2I 3.3 Å, Cryo-EM structure of the complex CDK16:CCNY:14-3-3

Browse structure collections

About this viewer

MolViewer shows 9R2N 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.