3u9x

X-ray diffraction
1.8Å resolution

Covalent attachment of pyridoxal-phosphate derivatives to 14-3-3 proteins

Released:
Source organism: Homo sapiens
Primary publication:
Covalent attachment of pyridoxal-phosphate derivatives to 14-3-3 proteins.
Proc. Natl. Acad. Sci. U.S.A. 109 E1051-3; author reply E1054 (2012)
PMID: 22532669

Function and Biology Details

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 Chain: A
Molecule details ›
Chain: A
Length: 235 amino acids
Theoretical weight: 26.73 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P31947 (Residues: 1-231; Coverage: 93%)
Gene names: HME1, SFN
Sequence domains: 14-3-3 protein
Structure domains: 14-3-3 domain

Ligands and Environments

3 bound ligands:
2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: C2221
Unit cell:
a: 82.22Å b: 112.14Å c: 62.66Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.156 0.133 0.188
Expression system: Escherichia coli BL21(DE3)