› 1u9h

X-ray diffraction
2.17Å resolution

Heterocyclic Peptide Backbone Modification in GCN4-pLI Based Coiled Coils: Replacement of E(22)L(23)

Released:
DOI: 10.2210/pdb1u9h/pdb
PDB entry 1u9h coloured by chain, front view.
PDB entry 1u9h coloured by chain, side view.
PDB entry 1u9h coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Heterocyclic peptide backbone modifications in an alpha-helical coiled coil.
Horne WS, Yadav MK, Stout CD, Ghadiri MR
J Am Chem Soc 126 15366-7 (2004)
PMID: 15563148

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162499 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
General control protein GCN4 Chains: A, B
Molecule details ›
Chains: A, B
Length: 33 amino acids
Theoretical weight: 4.02 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:
Ligand TA4 2 x TA4

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P4322
Unit cell:
a: 45.404Å b: 45.404Å c: 90.923Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.249 0.247 0.284
Expression system: Not provided

Quick links

Citations

17 review citations

Chemoselective ligation and modification strategies for peptides and proteins.
Hackenberger et al. (2008)
16 more

1 mention without citation

Heterocyclic peptide backbone modifications in an alpha-helical coiled coil.
Horne et al. (2004)