Sodium in PDB 5fb9: S1 Nuclease From Aspergillus Oryzae with Unoccupied Active Site

All present enzymatic activity of S1 Nuclease From Aspergillus Oryzae with Unoccupied Active Site:
3.1.30.1;

The structure of S1 Nuclease From Aspergillus Oryzae with Unoccupied Active Site, PDB code: 5fb9 was solved by T.Koval, L.H.Oestergaard, J.Dohnalek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.05 / 1.50
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	43.184, 48.595, 65.469, 107.37, 90.13, 105.72
R / Rfree (%)	14.9 / 17.7

The structure of S1 Nuclease From Aspergillus Oryzae with Unoccupied Active Site also contains other interesting chemical elements:

Zinc

(Zn)

6 atoms

The binding sites of Sodium atom in the S1 Nuclease From Aspergillus Oryzae with Unoccupied Active Site (pdb code 5fb9). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the S1 Nuclease From Aspergillus Oryzae with Unoccupied Active Site, PDB code: 5fb9:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the S1 Nuclease From Aspergillus Oryzae with Unoccupied Active Site


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of S1 Nuclease From Aspergillus Oryzae with Unoccupied Active Site within 5.0Å range: probe atom residue distance (Å) B Occ A:Na701 b:26.6 occ:1.00 O A:HOH1281 2.3 32.6 1.0 O A:HOH1091 2.4 23.2 1.0 O A:LEU118 2.7 17.9 1.0 C A:LEU118 3.8 16.6 1.0 O A:HOH1358 4.1 28.5 1.0 CA A:LEU118 4.5 14.6 1.0 NE2 A:GLN285 4.5 22.4 1.0 O A:HOH1247 4.6 37.6 1.0 O A:HOH1136 4.6 23.1 1.0 CB A:LEU118 4.7 14.5 1.0 O A:HOH1130 4.7 24.6 1.0 O A:HOH1410 4.7 33.6 1.0 N A:GLU119 4.9 18.2 1.0

Sodium binding site 2 out of 2 in the S1 Nuclease From Aspergillus Oryzae with Unoccupied Active Site


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of S1 Nuclease From Aspergillus Oryzae with Unoccupied Active Site within 5.0Å range: probe atom residue distance (Å) B Occ B:Na701 b:24.1 occ:1.00 O B:HOH1329 2.3 18.3 0.5 O B:HOH1321 2.3 15.9 0.5 O B:HOH1028 2.3 31.6 1.0 O B:HOH1280 2.5 20.4 0.5 O B:HOH1408 2.5 25.4 0.5 O B:ASN122 2.6 30.3 1.0 O B:HOH1388 3.5 26.2 0.5 O B:HOH1320 3.6 22.9 0.5 C B:ASN122 3.6 27.6 1.0 CA B:ASN122 4.0 26.4 1.0 CB B:ASN122 4.1 26.0 1.0 O B:HOH1089 4.2 40.8 1.0 O B:HOH1019 4.3 29.8 1.0 N B:GLY123 4.8 25.6 1.0 OD1 B:ASN122 4.9 30.8 1.0 O B:HOH1324 4.9 42.9 1.0 CG B:ASN122 4.9 28.5 1.0 O B:HOH1346 5.0 24.6 1.0

T.Koval, L.H.Stergaard, J.Lehmbeck, A.Nrgaard, P.Lipovova, J.Duskova, T.Skalova, M.Trundova, P.Kolenko, K.Fejfarova, J.Stransky, L.Svecova, J.Hasek, J.Dohnalek. Structural and Catalytic Properties of S1 Nuclease From Aspergillus Oryzae Responsible For Substrate Recognition, Cleavage, Non-Specificity, and Inhibition. Plos One V. 11 68832 2016.
ISSN: ESSN 1932-6203
PubMed: 28036383
DOI: 10.1371/JOURNAL.PONE.0168832