› 1zim

X-ray diffraction
2Å resolution

GCN4-LEUCINE ZIPPER CORE MUTANT ASN16GLN IN THE TRIMERIC STATE

Released:
DOI: 10.2210/pdb1zim/pdb
PDB entry 1zim coloured by chain, front view.
PDB entry 1zim coloured by chain, side view.
PDB entry 1zim coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Buried polar residues and structural specificity in the GCN4 leucine zipper.
Gonzalez L, Woolfson DN, Alber T
Nat Struct Biol 3 1011-8 (1996)
PMID: 8946854

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136531 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
General control transcription factor GCN4 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 34 amino acids
Theoretical weight: 4.05 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
Spacegroup: P212121
Unit cell:
a: 36.24Å b: 46.61Å c: 50.83Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.178 not available
Expression system: Not provided

Quick links

Citations

12 review citations

Coiled coil domains: stability, specificity, and biological implications.
Mason et al. (2004)
11 more

3 mentions without citation

A conserved trimerization motif controls the topology of short coiled coils.
Kammerer et al. (2005)
2 more