› 4tl1

X-ray diffraction
1.8Å resolution

GCN4-p1 with mutation to 1-Aminocyclohexanecarboxylic acid at residue 10

Released:
DOI: 10.2210/pdb4tl1/pdb
PDB entry 4tl1 coloured by chain, front view.
PDB entry 4tl1 coloured by chain, side view.
PDB entry 4tl1 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Origins of structural flexibility in protein-based supramolecular polymers revealed by DEER spectroscopy.
Tavenor NA, Silva KI, Saxena S, Horne WS
J Phys Chem B 118 9881-9 (2014)
PMID: 25060334

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: 35 amino acids
Theoretical weight: 4.03 KDa
Source organism: Saccharomyces cerevisiae S288C
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

1 bound ligand:
Ligand IPA 1 x IPA
1 modified residue:
Ligand 02K 2 x 02K

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: C2
Unit cell:
a: 83.322Å b: 30.35Å c: 28.019Å
α: 90° β: 101.68° γ: 90°
R-values:
R R work R free
0.187 0.185 0.228
Expression system: Not provided

Quick links

Citations

3 citation in other articles

Conformational Changes Underlying Desensitization of the Pentameric Ligand-Gated Ion Channel ELIC.
Kinde et al. (2015)
2 more

2 mentions without citation

Nuclear Magnetic Resonance Structures of GCN4p Are Largely Conserved When Ion Pairs Are Disrupted at Acidic pH but Show a Relaxation of the Coiled Coil Superhelix.
Kaplan et al. (2017)
1 more