› 4dmd

X-ray diffraction
2Å resolution

GCN4 leucine zipper domain in a dimeric oligomerization state

Released:
DOI: 10.2210/pdb4dmd/pdb
PDB entry 4dmd coloured by chain, front view.
PDB entry 4dmd coloured by chain, side view.
PDB entry 4dmd coloured by chain, top view.
Source organism: synthetic construct
Primary publication:
The native GCN4 leucine-zipper domain does not uniquely specify a dimeric oligomerization state.
Oshaben KM, Salari R, McCaslin DR, Chong LT, Horne WS
Biochemistry 51 9581-91 (2012)
PMID: 23116373

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136527 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
General control transcription factor GCN4 Chains: A, B
Molecule details ›
Chains: A, B
Length: 34 amino acids
Theoretical weight: 4.03 KDa
Source organism: synthetic construct
Expression system: Not provided
UniProt:
  • Canonical: P03069 (Residues: 249-281; Coverage: 12%)
Gene names: AAS101, AAS3, ARG9, GCN4, YEL009C
Sequence domains: Basic region leucine zipper

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: C2
Unit cell:
a: 83.449Å b: 30.478Å c: 27.816Å
α: 90° β: 104.48° γ: 90°
R-values:
R R work R free
0.237 0.235 0.265
Expression system: Not provided

Quick links

Citations

4 review citations

Assessing the accuracy of physical models used in protein-folding simulations: quantitative evidence from long molecular dynamics simulations.
Piana et al. (2014)
3 more

8 mentions without citation

The native GCN4 leucine-zipper domain does not uniquely specify a dimeric oligomerization state.
Oshaben et al. (2012)
7 more