1b2s

X-ray diffraction
1.82Å resolution

STRUCTURAL RESPONSE TO MUTATION AT A PROTEIN-PROTEIN INTERFACE

Released:
Source organism: Bacillus amyloliquefaciens
Primary publication:
Structural response to mutation at a protein-protein interface.
J Mol Biol 286 1487-506 (1999)
PMID: 10064711

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-132803 (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: 12.34 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: D, E, F
Molecule details ›
Chains: D, E, F
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

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: C2
Unit cell:
a: 206.24Å b: 43.51Å c: 83.69Å
α: 90° β: 107.42° γ: 90°
R-values:
R R work R free
0.194 0.194 0.249
Expression system: Escherichia coli