› 4ozb

X-ray diffraction
1.8Å resolution

Backbone Modifications in the Protein GB1 Helix: beta-ACPC24, beta-3-Lys28, beta-3-Lys31, beta-ACPC35

Released:
DOI: 10.2210/pdb4ozb/pdb
PDB entry 4ozb coloured by chain, front view.
PDB entry 4ozb coloured by chain, side view.
PDB entry 4ozb coloured by chain, top view.
Source organism: Streptococcus sp.
Primary publication:
Folding Thermodynamics of Protein-Like Oligomers with Heterogeneous Backbones.
Reinert ZE, Horne WS
Chem Sci 5 3325-3330 (2014)
PMID: 25071931

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148791 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Immunoglobulin G-binding protein G Chains: A, B
Molecule details ›
Chains: A, B
Length: 57 amino acids
Theoretical weight: 6.25 KDa
Source organism: Streptococcus sp.
Expression system: Not provided
UniProt:
  • Canonical: P19909 (Residues: 302-357; Coverage: 10%)
Gene name: spg
Sequence domains: B domain
Structure domains: Ubiquitin-like (UB roll)

Ligands and Environments

1 bound ligand:
Ligand GOL 2 x GOL
1 modified residue:
Ligand B3K 4 x B3K

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: C2
Unit cell:
a: 92.496Å b: 22.622Å c: 64.523Å
α: 90° β: 120.93° γ: 90°
R-values:
R R work R free
0.192 0.19 0.21
Expression system: Not provided

Quick links

Citations

2 review citations

Folding and function in α/β-peptides: targets and therapeutic applications.
Werner et al. (2015)
1 more

5 mentions without citation

Protein backbone engineering as a strategy to advance foldamers toward the frontier of protein-like tertiary structure.
Reinert et al. (2014)
4 more