› 5fba

X-ray diffraction
1.8Å resolution

Function and Biology Details

Reaction catalysed: 
Endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-phosphooligonucleotide end-products
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150145 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nuclease S1 Chain: A
Molecule details ›
Chain: A
Length: 267 amino acids
Theoretical weight: 29.08 KDa
Source organism: Aspergillus oryzae RIB40
Expression system: Aspergillus oryzae
UniProt:
  • Canonical: P24021 (Residues: 21-287; Coverage: 100%)
Gene names: AO090001000075, nucS
Sequence domains: S1/P1 Nuclease
Structure domains: P1 Nuclease

Ligands and Environments

4 bound ligands:
Ligand NAG 1 x NAG
Ligand ZN 3 x ZN
Ligand PO4 1 x PO4
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P21
Unit cell:
a: 41.765Å b: 62.307Å c: 48.003Å
α: 90° β: 106.75° γ: 90°
R-values:
R R work R free
0.153 0.152 0.199
Expression system: Aspergillus oryzae

Quick links

Citations

1 review citation

Site-Selective Artificial Ribonucleases: Renaissance of Oligonucleotide Conjugates for Irreversible Cleavage of RNA Sequences.
Staroseletz et al. (2021)
3 other articles

2 mentions without citation

Mechanistic Studies of Homo- and Heterodinuclear Zinc Phosphoesterase Mimics: What Has Been Learned?
Erxleben A. (2019)
1 more