› 1pyl

X-ray diffraction
1.51Å resolution

Crystal structure of Ribonuclease Sa2

Released:
DOI: 10.2210/pdb1pyl/pdb
PDB entry 1pyl coloured by chain, front view.
PDB entry 1pyl coloured by chain, side view.
PDB entry 1pyl coloured by chain, top view.
Source organism: Kitasatospora aureofaciens
Primary publication:
Crystal structure reveals two alternative conformations in the active site of ribonuclease Sa2.
Sevcík J, Dauter Z, Wilson KS
Acta Crystallogr D Biol Crystallogr 60 1198-204 (2004)
PMID: 15213380

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-176074 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease Chains: A, B
Molecule details ›
Chains: A, B
Length: 97 amino acids
Theoretical weight: 10.91 KDa
Source organism: Kitasatospora aureofaciens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q53752 (Residues: 67-163; Coverage: 60%)
Gene names: HS99_0012425, ribonuclease
Sequence domains: ribonuclease
Structure domains: Microbial ribonucleases

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 84.98Å b: 34.13Å c: 72.27Å
α: 90° β: 109.5° γ: 90°
R-values:
R R work R free
0.15 0.149 0.172
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Structure of RNase Sa2 complexes with mononucleotides--new aspects of catalytic reaction and substrate recognition.
Bauerová-Hlinková et al. (2009)

4 mentions without citation

Increasing protein stability by improving beta-turns.
Fu et al. (2009)
3 more