3UBW: 14-3-3 protein epsilon

Complex of 14-3-3 isoform epsilon, a Mlf1 phosphopeptide and a small fragment hit from a FBDD screen. Determined by X-ray diffraction at 1.9 Å resolution. Released 25 Jan 2012.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,184
Mol. weight: 32.26 kDa
Ligands: TBU, 6SP
Released: 25 Jan 2012

Explore 3UBW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3UBW contains 13 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: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	4-16	13
α-helix	20-31	12
α-helix	36-38	3
α-helix	39-71	33
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	214-231	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein epsilon	A	protein	261	Homo sapiens	P62258 (AlphaFold model)
Myeloid leukemia factor 1	P	protein	14	Homo sapiens	P58340 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3UBW_1 14-3-3 protein epsilon (chains A)
MSYHHHHHHDYDIPTTENLYFQGAMGSMDDREDLVYQAKLAEQAERYDEMVESMKKVAGM
DVELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEENKGGEDKLKMIREYRQMVETEL
KLICCDILDVLDKHLIPAANTGESKVFYYKMKGDYHRYLAEFATGNDRKEAAENSLVAYK
AASDIAMTELPPTHPIRLGLALNFSVFYYEILNSPDRACRLAKAAFDDAIAELDTLSEES
YKDSTLIMQLLRDNLTLWTSD

Sequence of entity 2 (P), FASTA

>3UBW_2 Myeloid leukemia factor 1 (chains P)
MIRSFSEPFGRDLL

Ligands and cofactors

ID	Name	Formula	Copies
TBU	Tertiary-butyl alcohol	C4 H10 O	5
6SP	(3S)-pyrrolidin-3-ol	C4 H9 N O	1

Primary citation

Structural insights of the MLF1/14-3-3 interaction. Molzan, M., Weyand, M., Rose, R. et al. FEBS J (2012) 279:563-571. DOI 10.1111/j.1742-4658.2011.08445.x · 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
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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