› 3o49

X-ray diffraction
1.45Å resolution

Crystal structure of Symfoil-1: de novo designed beta-trefoil architecture with symmetric primary structure

Released:
DOI: 10.2210/pdb3o49/pdb
PDB 3o49 coloured by chain and viewed from the front.
PDB 3o49 coloured by chain and viewed from the side.
PDB 3o49 coloured by chain and viewed from the top.
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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (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: 15.74 KDa
Source organism: synthetic construct
Expression system: Escherichia coli
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: I222
Unit cell:
a: 50.365Å b: 53.351Å c: 85.175Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.196 0.227
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Designing repeat proteins: a modular approach to protein design.
Parmeggiani et al. (2017)
10 more

1 mention without citation

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