› 1bao

X-ray diffraction
2.2Å resolution

THE CONTRIBUTION OF BURIED HYDROGEN BONDS TO PROTEIN STABILITY: THE CRYSTAL STRUCTURES OF TWO BARNASE MUTANTS

Released:
DOI: 10.2210/pdb1bao/pdb
PDB entry 1bao coloured by chain, front view.
PDB entry 1bao coloured by chain, side view.
PDB entry 1bao coloured by chain, top view.
Source organism: Bacillus amyloliquefaciens
Primary publication:
Contribution of buried hydrogen bonds to protein stability. The crystal structures of two barnase mutants.
Chen YW, Fersht AR, Henrick K
J Mol Biol 234 1158-70 (1993)
PMID: 8263918

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: 12.38 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Not provided
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
Spacegroup: P32
Unit cell:
a: 58.809Å b: 58.809Å c: 81.902Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.152 not available not available
Expression system: Not provided

Quick links

Citations

2 review citations

Prediction of binding constants of protein ligands: a fast method for the prioritization of hits obtained from de novo design or 3D database search programs.
Böhm HJ. (1998)
1 more

1 mention without citation

Quantitative first principles calculations of protein circular dichroism in the near-ultraviolet.
Li et al. (2017)