› 4ncu

X-ray diffraction
1.11Å resolution

Foldon domain wild type

Released:
DOI: 10.2210/pdb4ncu/pdb
PDB entry 4ncu coloured by chain, front view.
PDB entry 4ncu coloured by chain, side view.
PDB entry 4ncu coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
Versatile C(3)-symmetric scaffolds and their use for covalent stabilization of the foldon trimer.
Berthelmann A, Lach J, Gräwert MA, Groll M, Eichler J
Org Biomol Chem 12 2606-14 (2014)
PMID: 24637609

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145168 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fibritin Chain: A
Molecule details ›
Chain: A
Length: 27 amino acids
Theoretical weight: 3.08 KDa
Source organism: Escherichia virus T4
Expression system: Not provided
UniProt:
  • Canonical: P10104 (Residues: 458-484; Coverage: 6%)
Gene name: wac

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P63
Unit cell:
a: 27.839Å b: 27.839Å c: 63.527Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.122 0.121 0.141
Expression system: Not provided

Quick links

Citations

1 review citation

Synthetic Peptides as Protein Mimics.
Groß et al. (2015)
7 other articles

3 mentions without citation

The Effects of Aβ1-42 Binding to the SARS-CoV-2 Spike Protein S1 Subunit and Angiotensin-Converting Enzyme 2.
Hsu et al. (2021)
2 more