› 1a19

X-ray diffraction
2.76Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145870 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Barstar Chains: A, B
Molecule details ›
Chains: A, B
Length: 90 amino acids
Theoretical weight: 10.32 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11540 (Residues: 1-90; Coverage: 100%)
Sequence domains: Barstar (barnase inhibitor)
Structure domains: Barstar-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: I41
Unit cell:
a: 104.182Å b: 104.182Å c: 36Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.203 0.292
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Validation of protein models derived from experiment.
Laskowski et al. (1998)
1 more

43 mentions without citation

Protonation and pK changes in protein-ligand binding.
Onufriev et al. (2013)
42 more