› 3mp9

X-ray diffraction
1.2Å resolution

Structure of Streptococcal protein G B1 domain at pH 3.0

Released:
DOI: 10.2210/pdb3mp9/pdb
PDB entry 3mp9 coloured by chain, front view.
PDB entry 3mp9 coloured by chain, side view.
PDB entry 3mp9 coloured by chain, top view.
Source organism: Streptococcus sp. 'group G'
Primary publication:
Structural origins of pH-dependent chemical shifts in the B1 domain of protein G.
Tomlinson JH, Green VL, Baker PJ, Williamson MP
Proteins 78 3000-16 (2010)
PMID: 20715051

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
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: 64 amino acids
Theoretical weight: 7.22 KDa
Source organism: Streptococcus sp. 'group G'
Expression system: Escherichia coli BL21(DE3)
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:
Ligand FMT 2 x FMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P32
Unit cell:
a: 34.81Å b: 34.81Å c: 71.788Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.15 0.148 0.181
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Contemporary NMR Studies of Protein Electrostatics.
Hass et al. (2015)
12 other articles

1 mention without citation

Optimization of rotamers prior to template minimization improves stability predictions made by computational protein design.
Davey et al. (2015)