› 4oza

X-ray diffraction
2.2Å resolution

Backbone Modifications in the Protein GB1 Helix: beta-3-Ala24, beta-3-Lys28, beta-3-Gln32, beta-3-Asp36

Released:
DOI: 10.2210/pdb4oza/pdb
PDB entry 4oza coloured by chain, front view.
PDB entry 4oza coloured by chain, side view.
PDB entry 4oza 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 Chain: A
Molecule details ›
Chain: A
Length: 57 amino acids
Theoretical weight: 6.24 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 IPA 1 x IPA
4 modified residues:
Ligand B3A 1 x B3A
Ligand B3K 1 x B3K
Ligand B3Q 1 x B3Q
Ligand B3D 1 x B3D

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: I41
Unit cell:
a: 65.944Å b: 65.944Å c: 21.896Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.234 0.233 0.26
Expression system: Not provided

Quick links

Citations

3 review citations

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

1 mention without citation

Folding Thermodynamics of Protein-Like Oligomers with Heterogeneous Backbones.
Reinert et al. (2014)