Sodium in PDB 8bgy: O-Methyltransferase PLU4890 in Complex with Sah and Aq-284A

The structure of O-Methyltransferase PLU4890 in Complex with Sah and Aq-284A, PDB code: 8bgy was solved by E.M.Huber, M.Groll, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.95
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	63.13, 77.26, 166.88, 90, 95.49, 90
R / Rfree (%)	20 / 22.1

The structure of O-Methyltransferase PLU4890 in Complex with Sah and Aq-284A also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Sodium atom in the O-Methyltransferase PLU4890 in Complex with Sah and Aq-284A (pdb code 8bgy). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the O-Methyltransferase PLU4890 in Complex with Sah and Aq-284A, PDB code: 8bgy:

Sodium binding site 1 out of 1 in the O-Methyltransferase PLU4890 in Complex with Sah and Aq-284A


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of O-Methyltransferase PLU4890 in Complex with Sah and Aq-284A within 5.0Å range: probe atom residue distance (Å) B Occ D:Na403 b:57.5 occ:1.00 O B:HOH501 2.3 44.0 1.0 OH D:TYR219 2.4 40.5 1.0 OD2 D:ASP205 2.7 40.9 1.0 NE2 D:HIS188 2.8 48.7 1.0 CZ D:TYR219 3.5 39.4 1.0 NH2 B:ARG165 3.5 37.4 1.0 CD2 D:HIS188 3.7 48.0 1.0 NH2 D:ARG165 3.7 46.6 1.0 CE1 D:HIS188 3.7 48.6 1.0 CG D:ASP205 3.8 39.9 1.0 NE2 B:HIS188 3.9 43.0 1.0 OD2 B:ASP205 3.9 47.2 1.0 CE2 D:TYR219 4.0 39.1 1.0 CB D:ALA190 4.2 36.1 1.0 CE1 B:HIS188 4.3 43.8 1.0 OH B:TYR219 4.3 42.8 1.0 CB D:ASP205 4.4 39.3 1.0 CE1 D:TYR219 4.5 38.8 1.0 CD1 D:ILE207 4.7 34.7 1.0 CZ B:ARG165 4.8 37.9 1.0 OD1 D:ASP205 4.8 40.2 1.0 ND1 D:HIS188 4.9 48.0 1.0 CD2 B:HIS188 4.9 43.1 1.0 CG D:HIS188 4.9 47.4 1.0 CZ D:ARG165 4.9 46.1 1.0 CG B:ASP205 4.9 45.9 1.0

E.M.Huber, L.Kreling, A.K.Heinrich, M.Duennebacke, A.Poethig, H.B.Bode, M.Groll. A Set of Closely Related Methyltransferases For Site-Specific Tailoring of Anthraquinone Pigments Structure 2023.
ISSN: ISSN 0969-2126