6u3w

X-ray diffraction
2.39Å resolution

Crystal structure of yeast alpha/epsilon-COP of the COPI vesicular coat

Released:
Primary publication:
Roles of singleton tryptophan motifs in COPI coat stability and vesicle tethering.
Proc Natl Acad Sci U S A 116 24031-24040 (2019)
PMID: 31712447

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-154131 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Coatomer subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 303 amino acids
Theoretical weight: 33.99 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P53622 (Residues: 899-1201; Coverage: 25%)
Gene names: COP1, D1578, RET1, SEC33, SOO1, YDL145C
Sequence domains: Coatomer (COPI) alpha subunit C-terminus
Coatomer subunit epsilon Chain: B
Molecule details ›
Chain: B
Length: 310 amino acids
Theoretical weight: 35.47 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P40509 (Residues: 1-296; Coverage: 100%)
Gene names: SEC28, YIL076W
Sequence domains: Coatomer epsilon subunit

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P212121
Unit cell:
a: 72.264Å b: 84.594Å c: 117.842Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.178 0.238
Expression system: Escherichia coli BL21