1ywt

X-ray diffraction
2.4Å resolution

Crystal structure of the human sigma isoform of 14-3-3 in complex with a mode-1 phosphopeptide

Released:
Source organism: Homo sapiens
Primary publication:
A structural basis for 14-3-3sigma functional specificity.
J. Biol. Chem. 280 18891-8 (2005)
PMID: 15731107

Function and Biology Details

Structure analysis Details

Assemblies composition:
hetero tetramer (preferred)
hetero octamer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
14-3-3 protein sigma Chains: A, B
Molecule details ›
Chains: A, B
Length: 248 amino acids
Theoretical weight: 27.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P31947 (Residues: 1-248; Coverage: 100%)
Gene names: HME1, SFN
Sequence domains: 14-3-3 protein
Structure domains: 14-3-3 domain
synthetic optimal phosphopeptide (mode-1) Chains: C, D
Molecule details ›
Chains: C, D
Length: 12 amino acids
Theoretical weight: 1.42 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 8-BM
Spacegroup: C2221
Unit cell:
a: 56.173Å b: 137.093Å c: 155.313Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.238 0.233 0.283
Expression systems:
  • Escherichia coli
  • Not provided