PDBe 1brs

X-ray diffraction
2Å resolution

PROTEIN-PROTEIN RECOGNITION: CRYSTAL STRUCTURAL ANALYSIS OF A BARNASE-BARSTAR COMPLEX AT 2.0-A RESOLUTION

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ribonuclease Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 110 amino acids
Theoretical weight: 12.4 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00648 (Residues: 48-157; Coverage: 89%)
Sequence domains: ribonuclease
Structure domains: Microbial ribonucleases
Barstar Chains: D, E, F
Molecule details ›
Chains: D, E, F
Length: 89 amino acids
Theoretical weight: 10.16 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11540 (Residues: 2-90; Coverage: 99%)
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
Spacegroup: C2
Unit cell:
a: 207.25Å b: 43.86Å c: 84.71Å
α: 90° β: 107.76° γ: 90°
R-values:
R R work R free
0.172 not available not available
Expression system: Escherichia coli