› 3rhu

X-ray diffraction
2.8Å resolution

Epitope backbone grafting by computational design for improved presentation of linear epitopes on scaffold proteins

Released:
DOI: 10.2210/pdb3rhu/pdb
PDB entry 3rhu coloured by chain, front view.
PDB entry 3rhu coloured by chain, side view.
PDB entry 3rhu coloured by chain, top view.
Source organism: Pyrococcus horikoshii OT3
Primary publication:
Computational design of high-affinity epitope scaffolds by backbone grafting of a linear epitope.
Azoitei ML, Ban YE, Julien JP, Bryson S, Schroeter A, Kalyuzhniy O, Porter JR, Adachi Y, Baker D, Pai EF, Schief WR
J Mol Biol 415 175-92 (2012)
PMID: 22061265

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-129701 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alanyl-tRNA editing protein AlaX-S Chains: A, B
Molecule details ›
Chains: A, B
Length: 160 amino acids
Theoretical weight: 18.19 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
UniProt:
  • Canonical: O58307 (Residues: 1-154; Coverage: 98%)
Gene names: PH0574, alaXS
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: I4
Unit cell:
a: 103.65Å b: 103.65Å c: 85.669Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.282 0.28 0.312
Expression system: Escherichia coli

Quick links

Citations

24 review citations

Modern subunit vaccines: development, components, and research opportunities.
Moyle et al. (2013)
23 more

3 mentions without citation

Strategies to control the binding mode of de novo designed protein interactions.
Der et al. (2013)
2 more