29II: 14-3-3 epsilon

Structure of 14-3-3 epsilon in complex with a peptide derived from AMPK gamma 2. Determined by X-ray diffraction at 2.17 Å resolution. Released 9 Sept 2026.

Method: X-ray diffraction
Resolution: 2.17 Å
Organism: Homo sapiens
Chains: 3
Atoms: 3,780
Mol. weight: 56.89 kDa
Released: 9 Sept 2026

Explore 29II in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

29II contains 25 α-helices and 0 β-strands across 2 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: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	4-17	14
α-helix	20-31	12
α-helix	36-38	3
α-helix	39-71	33
α-helix	77-103	27
α-helix	104-108	5
α-helix	109-111	3
α-helix	115-135	21
α-helix	138-162	25
α-helix	168-184	17
α-helix	188-203	16
α-helix	206-208	3
α-helix	211-231	21

Chain B: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	4-17	14
α-helix	20-31	12
α-helix	36-38	3
α-helix	39-72	34
α-helix	77-103	27
α-helix	104-108	5
α-helix	115-135	21
α-helix	138-162	25
α-helix	168-184	17
α-helix	188-203	16
α-helix	206-208	3
α-helix	211-231	21

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein epsilon	A, B	protein	231	Homo sapiens	P62258 (AlphaFold model)
Isoform C of 5'-AMP-activated protein kinase subunit gamma-2	C	protein	34	Homo sapiens

Sequence of entity 1 (A, B), FASTA

>29II_1 14-3-3 protein epsilon (chains A, B)
DREDLVYQAKLAEQAERYDEMVESMKKVAGMDVELTVEERNLLSVAYKNVIGARRASWRI
ISSIEQKEENKGGEDKLKMIREYRQMVETELKLICCDILDVLDKHLIPAANTGESKVFYY
KMKGDYHRYLAEFATGNDRKEAAENSLVAYKAASDIAMTELPPTHPIRLGLALNFSVFYY
EILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTS

Sequence of entity 2 (C), FASTA

>29II_2 Isoform C of 5'-AMP-activated protein kinase subunit gamma-2 (chains C)
VRPKTSPGSPKTVFPFSYQESPPRSPRRMSFSGI

Primary citation

Binding of 14-3-3 stabilises recombinant AMPK gamma 2-containing complexes. Chen, S.Y., Bennett, J., Navaratnam, N. et al. Biochem J (2026) 483:621-637. DOI 10.1042/BCJ20250342 · PubMed

Other PDB entries of the same protein (UniProt P62258 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2BR9 1.75 Å, 14-3-3 Protein Epsilon (Human) Complexed to Peptide
3UAL 1.8 Å, Crystal Structure of 14-3-3 epsilon with Mlf1 peptide
7V9B 1.85 Å, Crystal Structure of 14-3-3 epsilon with FOXO3a peptide
3UBW 1.9 Å, Complex of 14-3-3 isoform epsilon, a Mlf1 phosphopeptide and a small fragment hit from a…
6EIH 2.7 Å, The crystal structure of 14-3-3 epsilon in complex with the phosphorylated NELFE peptide
8DGP 2.7 Å, 14-3-3 epsilon bound to phosphorylated PEAK3 (pS69) peptide
8DP5 3.1 Å, Structure of the PEAK3/14-3-3 complex
7C8E 3.16 Å, Crystal Structure of 14-3-3 epsilon with 9J10 peptide
8DGN 3.16 Å, 14-3-3 epsilon bound to phosphorylated PEAK2 (pS826) peptide
8DGM 3.2 Å, 14-3-3 epsilon bound to phosphorylated PEAK1 (pT1165) peptide
8Q1S 3.23 Å, Pathogenic mutations of human phosphorylation sites affect protein-protein interactions

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