› 1pgb

X-ray diffraction
1.92Å resolution

TWO CRYSTAL STRUCTURES OF THE B1 IMMUNOGLOBULIN-BINDING DOMAIN OF STREPTOCCOCAL PROTEIN G AND COMPARISON WITH NMR

Released:
DOI: 10.2210/pdb1pgb/pdb
PDB entry 1pgb coloured by chain, front view.
PDB entry 1pgb coloured by chain, side view.
PDB entry 1pgb coloured by chain, top view.
Source organism: Streptococcus sp. GX7805
Primary publication:
Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR.
Gallagher T, Alexander P, Bryan P, Gilliland GL
Biochemistry 33 4721-9 (1994)
PMID: 8161530

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139123 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Immunoglobulin G-binding protein G Chain: A
Molecule details ›
Chain: A
Length: 56 amino acids
Theoretical weight: 6.2 KDa
Source organism: Streptococcus sp. GX7805
Expression system: Not provided
UniProt:
  • Canonical: P06654 (Residues: 228-282; Coverage: 13%)
Gene name: spg
Sequence domains: B domain
Structure domains: Ubiquitin-like (UB roll)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 36.633Å b: 36.633Å c: 79.254Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 not available not available
Expression system: Not provided

Quick links

Citations

7 review citations

From folding theories to folding proteins: a review and assessment of simulation studies of protein folding and unfolding.
Shea et al. (2001)
6 more

111 mentions without citation

The OPEP protein model: from single molecules, amyloid formation, crowding and hydrodynamics to DNA/RNA systems.
Sterpone et al. (2014)
110 more