› 3ogf

X-ray diffraction
2.86Å resolution

Crystal structure of Difoil-4P homo-trimer: de novo designed dimeric trefoil-fold sub-domain which forms homo-trimer assembly

Released:
DOI: 10.2210/pdb3ogf/pdb
PDB entry 3ogf coloured by chain, front view.
PDB entry 3ogf coloured by chain, side view.
PDB entry 3ogf 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:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163855 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
de novo designed dimeric trefoil-fold sub-domain which forms homo-trimer assembly Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 90 amino acids
Theoretical weight: 10.07 KDa
Source organism: synthetic construct
Expression system: Escherichia coli

Ligands and Environments

1 bound ligand:
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: I212121
Unit cell:
a: 81.242Å b: 85.414Å c: 86.086Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.231 0.227 0.311
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

2 mentions without citation

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