4kgr

X-ray diffraction
2Å resolution

Backbone Modifications in the Protein GB1 Helix: beta-3-Ala24, beta-3-Lys28, beta-3-Lys31, beta-3-Asn35

Released:
Source organism: Streptococcus sp. 'group G'
Primary publication:
Protein-like tertiary folding behavior from heterogeneous backbones.
J Am Chem Soc 135 12528-31 (2013)
PMID: 23937097

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-139123 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Immunoglobulin G-binding protein G Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 57 amino acids
Theoretical weight: 6.24 KDa
Source organism: Streptococcus sp. 'group G'
Expression system: Not provided
UniProt:
  • Canonical: P06654 (Residues: 227-282; Coverage: 14%)
Gene name: spg
Sequence domains: B domain
Structure domains: Ubiquitin-like (UB roll)

Ligands and Environments

1 bound ligand:
3 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P21
Unit cell:
a: 52.162Å b: 81.168Å c: 52.063Å
α: 90° β: 89.97° γ: 90°
R-values:
R R work R free
0.162 0.158 0.192
Expression system: Not provided