Sodium in PDB 8bic: O-Methyltransferase PLU4891 in Complex with Sah

The structure of O-Methyltransferase PLU4891 in Complex with Sah, PDB code: 8bic 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 / 1.85
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	172.28, 57.94, 97.18, 90, 121.78, 90
R / Rfree (%)	18.8 / 22.6

The binding sites of Sodium atom in the O-Methyltransferase PLU4891 in Complex with Sah (pdb code 8bic). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the O-Methyltransferase PLU4891 in Complex with Sah, PDB code: 8bic:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the O-Methyltransferase PLU4891 in Complex with Sah


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of O-Methyltransferase PLU4891 in Complex with Sah within 5.0Å range: probe atom residue distance (Å) B Occ A:Na402 b:35.2 occ:1.00 OD1 A:ASP275 2.4 20.2 1.0 O A:GLY280 2.8 15.7 1.0 NH1 B:ARG51 2.9 19.5 1.0 O A:LEU279 3.1 18.1 1.0 C A:LEU279 3.3 18.0 1.0 CG A:ASP275 3.5 17.9 1.0 CA A:LEU279 3.7 17.9 1.0 NH2 B:ARG51 3.7 18.0 1.0 C A:GLY280 3.8 16.6 1.0 CZ B:ARG51 3.8 18.4 1.0 N A:GLY280 3.9 17.2 1.0 CB A:ASP275 4.1 16.6 1.0 CA A:ASP275 4.1 16.0 1.0 CG B:ARG48 4.2 18.7 1.0 CD2 A:LEU279 4.2 20.7 1.0 CA A:GLY280 4.3 16.9 1.0 NE B:ARG48 4.3 20.3 1.0 CD B:ARG48 4.3 19.8 1.0 CB A:LEU279 4.3 19.9 1.0 CE A:LYS281 4.4 27.7 1.0 OD2 A:ASP275 4.4 18.3 1.0 O B:HOH569 4.5 25.9 1.0 CB A:LYS281 4.6 20.0 1.0 N A:LYS281 4.8 17.7 1.0 CG A:LEU279 4.9 20.1 1.0 N A:ASP275 5.0 15.1 1.0

Sodium binding site 2 out of 2 in the O-Methyltransferase PLU4891 in Complex with Sah


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of O-Methyltransferase PLU4891 in Complex with Sah within 5.0Å range: probe atom residue distance (Å) B Occ B:Na403 b:55.1 occ:1.00 O B:PHE18 2.1 18.1 1.0 OG B:SER24 2.5 38.1 1.0 N B:LEU23 3.0 27.2 1.0 C B:PHE18 3.1 16.9 1.0 N B:SER24 3.1 34.4 1.0 N B:GLY22 3.4 19.8 1.0 O B:VAL19 3.6 18.6 1.0 CA B:VAL19 3.7 17.4 1.0 CB B:SER24 3.7 37.1 1.0 N B:VAL19 3.8 17.5 1.0 C B:GLY22 3.8 24.6 1.0 CA B:LEU23 3.8 28.9 1.0 C B:VAL19 3.8 17.9 1.0 CA B:GLY22 3.9 22.1 1.0 O B:HOH533 3.9 30.5 1.0 C B:LEU23 3.9 30.9 1.0 CA B:SER24 3.9 35.3 1.0 CB B:LEU23 4.0 31.2 1.0 CD2 B:PHE18 4.1 18.7 1.0 CG B:PHE18 4.2 17.0 1.0 C B:MET21 4.2 20.0 1.0 CE2 B:PHE18 4.2 19.9 1.0 CA B:PHE18 4.3 16.4 1.0 CD1 B:PHE18 4.4 18.4 1.0 N B:MET21 4.4 20.0 1.0 CZ B:PHE18 4.5 18.2 1.0 CB B:MET21 4.5 22.1 1.0 CE1 B:PHE18 4.5 18.5 1.0 CA B:MET21 4.6 20.8 1.0 O B:HOH557 4.7 29.9 1.0 N B:ASP20 4.8 17.6 1.0 CB B:PHE18 4.8 16.1 1.0 CG B:LEU23 4.8 33.4 1.0 O B:GLY22 4.9 32.3 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