3ual

X-ray diffraction
1.8Å resolution

Crystal Structure of 14-3-3 epsilon with Mlf1 peptide

Released:
Source organism: Homo sapiens
Primary publication:
Structural insights of the MLF1/14-3-3 interaction.
FEBS J 279 563-71 (2012)
PMID: 22151054

Function and Biology Details

Structure analysis Details

Assemblies composition:
hetero tetramer
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-157674 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
14-3-3 protein epsilon Chain: A
Molecule details ›
Chain: A
Length: 232 amino acids
Theoretical weight: 26.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62258 (Residues: 1-232; Coverage: 91%)
Gene name: YWHAE
Sequence domains: 14-3-3 protein
Structure domains: 14-3-3 domain
Myeloid leukemia factor 1 Chain: P
Molecule details ›
Chain: P
Length: 14 amino acids
Theoretical weight: 1.75 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P58340 (Residues: 29-42; Coverage: 5%)
Gene name: MLF1

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: C2221
Unit cell:
a: 77.98Å b: 81.46Å c: 82.84Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.172 0.222
Expression systems:
  • Escherichia coli
  • Not provided