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UniProt P62258

14-3-3 protein epsilon (P62258)

14-3-3 protein epsilon (UniProt P62258): 13 experimental structures and 1 predicted model on GenesisL1, 2 ligands bound, 21 pockets. Binding sites, druggability and experiment against prediction (TM-score) in GL1X.

UniProt
P62258
Protein
14-3-3 protein epsilon
Experimental structures
13
Predicted models
1
Ligands
2
Pockets
21 · 5 records with a druggable one

Structures

14 records of P62258 in the MolNFT archive: 13 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
2BR914-3-3 Protein Epsilon (Human) Complexed to Peptidex-ray diffractionA——
2BR914-3-3 protein epsilon (human) complexed to peptidex-ray diffractionA——
3UALCrystal Structure of 14-3-3 epsilon with Mlf1 peptidex-ray diffractionA——
3UALCrystal structure of 14-3-3 epsilon with MLF1 peptidex-ray diffractionA——
3UBWComplex of 14-3-3 isoform epsilon, a Mlf1 phosphopeptide and a small fragment hit from a FBDD screenx-ray diffractionA——
3UBWComplex of 14-3-3 isoform epsilon, a MLF1 phosphopeptide and a small fragment hit from a fbdd screenx-ray diffractionA——
6EIHThe crystal structure of 14-3-3 epsilon in complex with the phosphorylated NELFE peptidex-ray diffractionA—3 (best 0.59)
6EIHThe crystal structure of 14-3-3 epsilon in complex with the phosphorylated nelfe peptidex-ray diffractionA——
7C8ECrystal structure of 14-3-3 epsilon with 9J10 peptidex-ray diffractionA, B——
8DGM14-3-3 epsilon bound to phosphorylated PEAK1 (pT1165) peptidex-ray diffractionA—3 (best 0.60)
8DGN14-3-3 epsilon bound to phosphorylated PEAK2 (pS826) peptidex-ray diffractionA—4 (best 0.60)
8DP5Structure of the PEAK3/14-3-3 complexelectron microscopyD—4 (best 0.84)
8Q1SPathogenic mutations of human phosphorylation sites affect protein-protein interactionsx-ray diffractionA, BBR, NA7 (best 0.70)
P62258AlphaFold monomer V2.0 prediction for 14-3-3 protein epsilon (P62258)predictedA——

Ligands

  • BR · Bromide ion · in 1 record
  • NA · Sodium ion · in 1 record

Experiment against prediction

Elsewhere

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