8DGP: 14-3-3 epsilon

14-3-3 epsilon bound to phosphorylated PEAK3 (pS69) peptide. Determined by X-ray diffraction at 2.7 Å resolution. Released 7 Jun 2023.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Homo sapiens
Chains: 8
Atoms: 7,663
Mol. weight: 128.21 kDa
Released: 7 Jun 2023

Explore 8DGP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8DGP contains 51 α-helices and 0 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.

Chain A: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	0-16	17
α-helix	20-31	12
α-helix	36-38	3
α-helix	39-73	35
α-helix	76-103	28
α-helix	104-108	5
α-helix	109-111	3
α-helix	115-135	21
α-helix	138-162	25
α-helix	168-183	16
α-helix	188-204	17
α-helix	206-208	3
α-helix	212-232	21

Chain B: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	3-17	15
α-helix	20-31	12
α-helix	36-38	3
α-helix	39-73	35
α-helix	76-103	28
α-helix	104-108	5
α-helix	109-111	3
α-helix	115-135	21
α-helix	138-162	25
α-helix	168-183	16
α-helix	188-204	17
α-helix	206-208	3
α-helix	211-232	22

Chain C: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	0-17	18
α-helix	20-31	12
α-helix	36-38	3
α-helix	39-73	35
α-helix	76-103	28
α-helix	104-108	5
α-helix	109-111	3
α-helix	115-135	21
α-helix	138-162	25
α-helix	168-183	16
α-helix	188-204	17
α-helix	211-233	23

Chain D: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	1-17	17
α-helix	20-31	12
α-helix	36-38	3
α-helix	39-73	35
α-helix	76-103	28
α-helix	104-108	5
α-helix	109-111	3
α-helix	115-135	21
α-helix	138-162	25
α-helix	168-183	16
α-helix	188-204	17
α-helix	206-208	3
α-helix	211-232	22

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein epsilon	A, B, C, D	protein	258	Homo sapiens	P62258 (AlphaFold model)
Phosphorylated PEAK3 (pS69) peptide	E, F, G, H	protein	21	Homo sapiens	Q6ZS72 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>8DGP_1 14-3-3 protein epsilon (chains A, B, C, D)
GSTMDDREDLVYQAKLAEQAERYDEMVESMKKVAGMDVELTVEERNLLSVAYKNVIGARR
ASWRIISSIEQKEENKGGEDKLKMIREYRQMVETELKLICCDILDVLDKHLIPAANTGES
KVFYYKMKGDYHRYLAEFATGNDRKEAAENSLVAYKAASDIAMTELPPTHPIRLGLALNF
SVFYYEILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDMQG
DGEEQNKEALQDVEDENQ

Sequence of entity 2 (E, F, G, H), FASTA

>8DGP_2 Phosphorylated PEAK3 (pS69) peptide (chains E, F, G, H)
PLPPPLPKKILTRTQSLPTRR

Primary citation

Structural mapping of PEAK pseudokinase interactions identifies 14-3-3 as a molecular switch for PEAK3 signaling. Roy, M.J., Surudoi, M.G., Kropp, A. et al. Nat Commun (2023) 14:3542-3542. DOI 10.1038/s41467-023-38869-9 · 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…
29II 2.17 Å, Structure of 14-3-3 epsilon in complex with a peptide derived from AMPK gamma 2
6EIH 2.7 Å, The crystal structure of 14-3-3 epsilon in complex with the phosphorylated NELFE 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

Browse structure collections

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