› 3d5g

X-ray diffraction
1.8Å resolution

Structure of ribonuclease Sa2 complexes with mononucleotides: new aspects of catalytic reaction and substrate recognition

Released:
DOI: 10.2210/pdb3d5g/pdb
PDB entry 3d5g coloured by chain, front view.
PDB entry 3d5g coloured by chain, side view.
PDB entry 3d5g coloured by chain, top view.
Source organism: Kitasatospora aureofaciens
Primary publication:
Structure of RNase Sa2 complexes with mononucleotides--new aspects of catalytic reaction and substrate recognition.
Bauerová-Hlinková V, Dvorský R, Perecko D, Povazanec F, Sevcík J
FEBS J 276 4156-68 (2009)
PMID: 19558492

Function and Biology Details

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

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, C
Molecule details ›
Chains: A, B, C
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 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X31
Spacegroup: C2
Unit cell:
a: 100.655Å b: 67.667Å c: 57.085Å
α: 90° β: 100.63° γ: 90°
R-values:
R R work R free
0.177 0.174 0.243
Expression system: Escherichia coli

Quick links

Citations

12 citation in other articles

The structural basis for mRNA recognition and cleavage by the ribosome-dependent endonuclease RelE.
Neubauer et al. (2009)
11 more

1 mention without citation

Predicting binding sites from unbound versus bound protein structures.
Clark et al. (2020)