› 1brh

X-ray diffraction
2Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132802 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 110 amino acids
Theoretical weight: 12.36 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00648 (Residues: 48-157; Coverage: 89%)
Sequence domains: ribonuclease
Structure domains: Microbial ribonucleases

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS
Spacegroup: P32
Unit cell:
a: 58.8Å b: 58.8Å c: 81.68Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.155 not available not available
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Structural biology of the tumor suppressor p53.
Joerger et al. (2008)
11 more

1 mention without citation

Interatomic potentials and solvation parameters from protein engineering data for buried residues.
Lomize et al. (2002)