6tzt

X-ray diffraction
3.06Å resolution

Crystal structure of human alpha/epsilon-COP of the COPI vesicular coat bound to alpha-COP STM2

Released:
Source organism: Homo sapiens
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

Assemblies composition:
hetero tetramer
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-127012 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Coatomer subunit epsilon Chains: A, C
Molecule details ›
Chains: A, C
Length: 322 amino acids
Theoretical weight: 36.14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O14579 (Residues: 1-308; Coverage: 100%)
Gene name: COPE
Sequence domains: Coatomer epsilon subunit
Coatomer subunit alpha Chains: B, D
Molecule details ›
Chains: B, D
Length: 356 amino acids
Theoretical weight: 39.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P53621 (Residues: 870-1224; Coverage: 29%)
Gene name: COPA
Sequence domains: Coatomer (COPI) alpha subunit C-terminus

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS-II BEAMLINE 17-ID-1
Spacegroup: P3121
Unit cell:
a: 138.47Å b: 138.47Å c: 192.868Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.178 0.222
Expression system: Escherichia coli BL21