PDBe 1ce9

X-ray diffraction
1.8Å resolution

HELIX CAPPING IN THE GCN4 LEUCINE ZIPPER

Released:
Source organism: Synthetic construct
Primary publication:
Helix capping in the GCN4 leucine zipper.
J. Mol. Biol. 288 743-52 (1999)
PMID: 10329176

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Structure domain:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
General control protein GCN4 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 34 amino acids
Theoretical weight: 4.04 KDa
Source organism: Synthetic construct
Expression system: Not provided
UniProt:
  • Canonical: P03069 (Residues: 250-281; Coverage: 11%)
Gene names: AAS3, ARG9, GCN4, YEL009C

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P1
Unit cell:
a: 28.304Å b: 30.769Å c: 42.884Å
α: 75.41° β: 79.76° γ: 90.08°
R-values:
R R work R free
0.214 0.214 0.283
Expression system: Not provided