› 1yz5

X-ray diffraction
2.8Å resolution

The crystal structure of 14-3-3-sigma at 2.8 angstrom resolution

Released:
DOI: 10.2210/pdb1yz5/pdb
PDB entry 1yz5 coloured by chain, front view.
PDB entry 1yz5 coloured by chain, side view.
PDB entry 1yz5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The crystal structure of the non-liganded 14-3-3sigma protein: insights into determinants of isoform specific ligand binding and dimerization.
Benzinger A, Popowicz GM, Joy JK, Majumdar S, Holak TA, Hermeking H
Cell Res 15 219-27 (2005)
PMID: 15857576

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152124 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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 BL21
UniProt:
  • Canonical: P31947 (Residues: 1-248; Coverage: 100%)
Gene names: HME1, SFN
Sequence domains: 14-3-3 protein
Structure domains: 14-3-3 domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P212121
Unit cell:
a: 71.65Å b: 80.85Å c: 99.13Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.219 0.292
Expression system: Escherichia coli BL21

Quick links

Citations

15 review citations

14-3-3 proteins: a historic overview.
Aitken A. (2006)
14 more

15 mentions without citation

14-3-3σ and Its Modulators in Cancer.
Aljabal et al. (2020)
14 more