› 4dme

X-ray diffraction
2.2Å resolution

GCN4 leucine zipper domain in a trimeric oligomerization state

Released:
DOI: 10.2210/pdb4dme/pdb
PDB entry 4dme coloured by chain, front view.
PDB entry 4dme coloured by chain, side view.
PDB entry 4dme 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 trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-164395 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GCN4-p1 leucine zipper domain Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 35 amino acids
Theoretical weight: 4.03 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: C2
Unit cell:
a: 61.179Å b: 34.379Å c: 78.117Å
α: 90° β: 139.68° γ: 90°
R-values:
R R work R free
0.229 0.226 0.287
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

5 mentions without citation

Structure of the meningococcal vaccine antigen NadA and epitope mapping of a bactericidal antibody.
Malito et al. (2014)
4 more