2za4

X-ray diffraction
1.58Å resolution

Crystal Structural Analysis of Barnase-barstar Complex

Released:

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
monomeric
PDBe Complex ID:
PDB-CPX-132803 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ribonuclease Chains: A, C
Molecule details ›
Chains: A, C
Length: 110 amino acids
Theoretical weight: 12.34 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: B, D
Molecule details ›
Chains: B, D
Length: 90 amino acids
Theoretical weight: 10.24 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

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: C2
Unit cell:
a: 97.388Å b: 110.255Å c: 47.272Å
α: 90° β: 114.97° γ: 90°
R-values:
R R work R free
0.199 0.199 0.2
Expression system: Escherichia coli