2BR9: 14-3-3 protein epsilon

14-3-3 Protein Epsilon (Human) Complexed to Peptide. Determined by X-ray diffraction at 1.75 Å resolution. Released 12 May 2005.

Method: X-ray diffraction
Resolution: 1.75 Å
Organism: HOMO SAPIENS
Chains: 2
Atoms: 2,014
Mol. weight: 27.74 kDa
Released: 12 May 2005

Explore 2BR9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2BR9 contains 14 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: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	4-17	14
α-helix	20-31	12
α-helix	36-38	3
α-helix	39-73	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	168-179	12
α-helix	180-184	5
α-helix	188-204	17
α-helix	206-208	3
α-helix	214-231	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein epsilon	A	protein	234	HOMO SAPIENS	P62258 (AlphaFold model)
Consensus peptide for 14-3-3 proteins	P	protein	7	HOMO SAPIENS

Sequence of entity 1 (A), FASTA

>2BR9_1 14-3-3 PROTEIN EPSILON (chains A)
SMDDREDLVYQAKLAEQAERYDEMVESMKKVAGMDVELTVEERNLLSVAYKNVIGARRAS
WRIISSIEQKEENKGGEDKLKMIREYRQMVETELKLICCDILDVLDKHLIPAANTGESKV
FYYKMKGDYHRYLAEFATGNDRKEAAENSLVAYKAASDIAMTELPPTHPIRLGLALNFSV
FYYEILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTS

Sequence of entity 2 (P), FASTA

>2BR9_2 CONSENSUS PEPTIDE FOR 14-3-3 PROTEINS (chains P)
RRQRSAP

Primary citation

Structural Basis for Protein-Protein Interactions in the 14-3-3 Protein Family. Yang, X., Lee, W.H., Sobott, F. et al. Proc Natl Acad Sci U S A (2006) 103:17237. DOI 10.1073/PNAS.0605779103 · PubMed

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

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
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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