› 6lji

X-ray diffraction
1.84Å resolution

X-ray structure of synthetic GB1 domain with mutations K10(DVA), T11V

Released:
DOI: 10.2210/pdb6lji/pdb
PDB entry 6lji coloured by chain, front view.
PDB entry 6lji coloured by chain, side view.
PDB entry 6lji coloured by chain, top view.
Source organism: Streptococcus sp. 'group G'
Primary publication:
Increasing protein stability by engineering the n → π* interaction at the β-turn.
Khatri B, Majumder P, Nagesh J, Penmatsa A, Chatterjee J
Chem Sci 11 9480-9487 (2020)
PMID: 34094214

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-139123 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Immunoglobulin G-binding protein G Chains: A, B
Molecule details ›
Chains: A, B
Length: 56 amino acids
Theoretical weight: 6.15 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

Ligands and Environments

No bound ligands
1 modified residue:
Ligand DVA 2 x DVA

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: C2
Unit cell:
a: 90.722Å b: 23.066Å c: 48.395Å
α: 90° β: 109.04° γ: 90°
R-values:
R R work R free
0.28 0.278 0.328
Expression system: Not provided

Quick links

Citations

7 citation in other articles

Hydrogen Bond and Geometry Effects of Thioamide Backbone Modifications.
Lampkin et al. (2021)
6 more

2 mentions without citation

Increasing protein stability by engineering the n → π* interaction at the β-turn.
Khatri et al. (2020)
1 more