› 3bvg

X-ray diffraction
2Å resolution

Manipulating the coupled folding and binding process drives affinity maturation in a protein-protein complex

Released:
DOI: 10.2210/pdb3bvg/pdb
PDB entry 3bvg coloured by chain, front view.
PDB entry 3bvg coloured by chain, side view.
PDB entry 3bvg coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Assessing energetic contributions to binding from a disordered region in a protein-protein interaction .
Cho S, Swaminathan CP, Bonsor DA, Kerzic MC, Guan R, Yang J, Kieke MC, Andersen PS, Kranz DM, Mariuzza RA, Sundberg EJ
Biochemistry 49 9256-68 (2010)
PMID: 20836565

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140943 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enterotoxin type C-3 Chain: A
Molecule details ›
Chain: A
Length: 237 amino acids
Theoretical weight: 27.55 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A0L5 (Residues: 28-266; Coverage: 99%)
Gene name: entC3
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P43212
Unit cell:
a: 42.7Å b: 42.7Å c: 287.142Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 0.213 0.276
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Applications of isothermal titration calorimetry in pure and applied research--survey of the literature from 2010.
Ghai et al. (2012)
8 other articles

1 mention without citation

Assessing energetic contributions to binding from a disordered region in a protein-protein interaction .
Cho et al. (2010)