› 5fb9

X-ray diffraction
1.5Å 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 Chains: A, B
Molecule details ›
Chains: A, B
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 ZN 6 x ZN
Ligand NAG 4 x NAG
Ligand BTB 2 x BTB
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Spacegroup: P1
Unit cell:
a: 43.184Å b: 48.595Å c: 65.469Å
α: 107.37° β: 90.13° γ: 105.72°
R-values:
R R work R free
0.15 0.149 0.177
Expression system: Aspergillus oryzae

Quick links

Citations

2 review citations

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

1 mention without citation

Structural and Catalytic Properties of S1 Nuclease from Aspergillus oryzae Responsible for Substrate Recognition, Cleavage, Non-Specificity, and Inhibition.
Kovaľ et al. (2016)