6EIH: 14-3-3 epsilon

The crystal structure of 14-3-3 epsilon in complex with the phosphorylated NELFE peptide. Determined by X-ray diffraction at 2.7 Å resolution. Released 14 Feb 2018.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Homo sapiens
Chains: 2
Atoms: 1,859
Mol. weight: 26.91 kDa
Released: 14 Feb 2018

Explore 6EIH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6EIH contains 12 α-helices and 0 β-strands across 1 chain. 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	4-16	13
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	115-135	21
α-helix	138-162	25
α-helix	168-183	16
α-helix	188-203	16
α-helix	206-208	3
α-helix	214-230	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein epsilon	A	protein	230	Homo sapiens	P62258 (AlphaFold model)
Ser-ile-sep-arg	P	protein	4	Homo sapiens

Sequence of entity 1 (A), FASTA

>6EIH_1 14-3-3 protein epsilon (chains A)
DREDLVYQAKLAEQAERYDEMVESMKKVAGMDVELTVEERNLLSVAYKNVIGARRASWRI
ISSIEQKEENKGGEDKLKMIREYRQMVETELKLICCDILDVLDKHLIPAANTGESKVFYY
KMKGDYHRYLAEFATGNDRKEAAENSLVAYKAASDIAMTELPPTHPIRLGLALNFSVFYY
EILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWT

Sequence of entity 2 (P), FASTA

>6EIH_2 SER-ILE-SEP-ARG (chains P)
SISR

Primary citation

p38-MK2 signaling axis regulates RNA metabolism after UV-light-induced DNA damage. Borisova, M.E., Voigt, A., Tollenaere, M.A.X. et al. Nat Commun (2018) 9:1017-1017. DOI 10.1038/s41467-018-03417-3 · 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
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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