› 6ne4

X-ray diffraction
1.65Å resolution

Designed repeat protein specifically in complex with Fz7CRD

Released:
DOI: 10.2210/pdb6ne4/pdb
PDB entry 6ne4 coloured by chain, front view.
PDB entry 6ne4 coloured by chain, side view.
PDB entry 6ne4 coloured by chain, top view.
Source organisms:
Primary publication:
Receptor subtype discrimination using extensive shape complementary designed interfaces.
Dang LT, Miao Y, Ha A, Yuki K, Park K, Janda CY, Jude KM, Mohan K, Ha N, Vallon M, Yuan J, Vilches-Moure JG, Kuo CJ, Garcia KC, Baker D
Nat Struct Mol Biol 26 407-414 (2019)
PMID: 31086346

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130829 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Designed repeat binding protein Chain: B
Molecule details ›
Chain: B
Length: 200 amino acids
Theoretical weight: 20.96 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
Structure domains: Ankyrin repeat-containing domain
Frizzled-7 Chain: A
Molecule details ›
Chain: A
Length: 124 amino acids
Theoretical weight: 14.11 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: O75084 (Residues: 46-163; Coverage: 22%)
Gene name: FZD7
Sequence domains: Fz domain

Ligands and Environments

2 bound ligands:
Ligand SO4 14 x SO4
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Unit cell:
a: 57.604Å b: 68.367Å c: 86.468Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.16 0.186
Expression systems:
  • Escherichia coli
  • Trichoplusia ni

Quick links

Citations

3 review citations

Protein Assembly by Design.
Zhu et al. (2021)
2 more

1 mention without citation

Receptor subtype discrimination using extensive shape complementary designed interfaces.
Dang et al. (2019)