› 2bni

X-ray diffraction
1.5Å resolution

pLI mutant E20C L16G Y17H, antiparallel

Released:
DOI: 10.2210/pdb2bni/pdb
PDB entry 2bni coloured by chain, front view.
PDB entry 2bni coloured by chain, side view.
PDB entry 2bni coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structure-based engineering of internal cavities in coiled-coil peptides.
Yadav MK, Redman JE, Leman LJ, Alvarez-Gutiérrez JM, Zhang Y, Stout CD, Ghadiri MR
Biochemistry 44 9723-32 (2005)
PMID: 16008357

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136532 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
General control transcription factor GCN4 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 34 amino acids
Theoretical weight: 4.1 KDa
Source organism: Saccharomyces cerevisiae
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: APS BEAMLINE 23-ID-D
Spacegroup: P31
Unit cell:
a: 25.814Å b: 25.814Å c: 148.595Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.239 0.237 0.276
Expression system: Not provided

Quick links

Citations

2 review citations

Molecular recognition with designed peptides and proteins.
Cooper et al. (2005)
1 more

4 mentions without citation

What lessons can be learned from studying the folding of homologous proteins?
Nickson et al. (2010)
3 more