› 3o4d

X-ray diffraction
1.65Å resolution

Crystal structure of Symfoil-4P: de novo designed beta-trefoil architecture with symmetric primary structure

Released:
DOI: 10.2210/pdb3o4d/pdb
PDB entry 3o4d coloured by chain, front view.
PDB entry 3o4d coloured by chain, side view.
PDB entry 3o4d coloured by chain, top view.
Source organism: synthetic construct
Primary publication:
Experimental support for the evolution of symmetric protein architecture from a simple peptide motif.
Lee J, Blaber M
Proc Natl Acad Sci U S A 108 126-30 (2011)
PMID: 21173271

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163844 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
de novo designed beta-trefoil architecture with symmetric primary structure Chain: A
Molecule details ›
Chain: A
Length: 142 amino acids
Theoretical weight: 15.86 KDa
Source organism: synthetic construct
Expression system: Escherichia coli
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

Ligands and Environments

3 bound ligands:
Ligand TRS 1 x TRS
Ligand SO4 2 x SO4
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: I222
Unit cell:
a: 50.372Å b: 53.151Å c: 84.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.19 0.226
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Protein comparability assessments and potential applicability of high throughput biophysical methods and data visualization tools to compare physical stability profiles.
Alsenaidy et al. (2014)
12 more

7 mentions without citation

Experimental support for the evolution of symmetric protein architecture from a simple peptide motif.
Lee et al. (2011)
6 more