› 3ol0

X-ray diffraction
1.48Å resolution

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

Released:
DOI: 10.2210/pdb3ol0/pdb
PDB entry 3ol0 coloured by chain, front view.
PDB entry 3ol0 coloured by chain, side view.
PDB entry 3ol0 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 domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163860 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
de novo designed monomer trefoil-fold sub-domain which forms homo-trimer assembly Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 48 amino acids
Theoretical weight: 5.44 KDa
Source organism: synthetic construct
Expression system: Escherichia coli
Structure domains: SH3 type barrels.

Ligands and Environments

1 bound ligand:
Ligand SO4 5 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P212121
Unit cell:
a: 49.52Å b: 53.478Å c: 65.868Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.18 0.204
Expression system: Escherichia coli

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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

4 mentions without citation

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