› 1ij2

X-ray diffraction
1.7Å resolution

GCN4-pVTL Coiled-coil Trimer with Threonine at the a(16) position

Released:
DOI: 10.2210/pdb1ij2/pdb
PDB 1ij2 coloured by chain and viewed from the front.
PDB 1ij2 coloured by chain and viewed from the side.
PDB 1ij2 coloured by chain and viewed from the top.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Buried polar residues in coiled-coil interfaces.
Akey DL, Malashkevich VN, Kim PS
Biochemistry 40 6352-60 (2001)
PMID: 11371197

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
General control protein GCN4 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 34 amino acids
Theoretical weight: 4.02 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Not provided
UniProt:
  • Canonical: P03069 (Residues: 249-281; Coverage: 12%)
Gene names: AAS3, ARG9, GCN4, YEL009C

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P212121
Unit cell:
a: 35.763Å b: 46.332Å c: 51.359Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.243 0.243 0.279
Expression system: Not provided

Quick links

Citations

5 review citations

De Novo Designed α-Helical Coiled-Coil Peptides as Scaffolds for Chemical Reactions.
Rink et al. (2019)
4 more

1 mention without citation

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