7C8E: 14-3-3 epsilon with 9J10 peptide

Crystal Structure of 14-3-3 epsilon with 9J10 peptide. Determined by X-ray diffraction at 3.16 Å resolution. Released 2 Jun 2021.

Method: X-ray diffraction
Resolution: 3.16 Å
Organisms: Homo sapiens, Streptomyces avermitilis MA-4680 = NBRC 14893
Chains: 4
Atoms: 3,735
Mol. weight: 63.51 kDa
Released: 2 Jun 2021

Explore 7C8E in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7C8E contains 23 α-helices and 0 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: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	4-17	14
α-helix	20-31	12
α-helix	39-71	33
α-helix	79-103	25
α-helix	104-108	5
α-helix	115-135	21
α-helix	139-162	24
α-helix	168-183	16
α-helix	188-205	18
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	39-69	31
α-helix	78-103	26
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	188-202	15
α-helix	204-208	5
α-helix	211-230	20

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	7-10	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein epsilon	A, B	protein	266	Homo sapiens	P62258 (AlphaFold model)
9J10	C, D	protein	12	Streptomyces avermitilis MA-4680 = NBRC 14893

Sequence of entity 1 (A, B), FASTA

>7C8E_1 14-3-3 protein epsilon (chains A, B)
MGSSHHHHHHSSGLVPRGSHMASMTGGQQMGRGSMDDREDLVYQAKLAEQAERYDEMVES
MKKVAGMDVELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEENKGGEDKLKMIREYR
QMVETELKLICCDILDVLDKHLIPAANTGESKVFYYKMKGDYHRYLAEFATGNDRKEAAE
NSLVAYKAASDIAMTELPPTHPIRLGLALNFSVFYYEILNSPDRACRLAKAAFDDAIAEL
DTLSEESYKDSTLIMQLLRDNLTLWT

Sequence of entity 2 (C, D), FASTA

>7C8E_2 9J10 (chains C, D)
LNRTPGRRRNSN

Primary citation

Target identification for small-molecule discovery in the FOXO3a tumor-suppressor pathway using a biodiverse peptide library. Emery, A., Hardwick, B.S., Crooks, A.T. et al. Cell Chem Biol (2021) 28:1602-1615.e9. DOI 10.1016/j.chembiol.2021.05.009 · 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
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
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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