Magnesium in PDB 8iaa: Spnk Methyltransferase From the Spinosyn Biosynthetic Pathway in Complex with Sah

The structure of Spnk Methyltransferase From the Spinosyn Biosynthetic Pathway in Complex with Sah, PDB code: 8iaa was solved by S.Huang, J.Zheng, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.63 / 2.10
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	133.975, 133.975, 160.109, 90, 90, 90
R / Rfree (%)	20.1 / 22.8

The binding sites of Magnesium atom in the Spnk Methyltransferase From the Spinosyn Biosynthetic Pathway in Complex with Sah (pdb code 8iaa). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Spnk Methyltransferase From the Spinosyn Biosynthetic Pathway in Complex with Sah, PDB code: 8iaa:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Spnk Methyltransferase From the Spinosyn Biosynthetic Pathway in Complex with Sah


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Spnk Methyltransferase From the Spinosyn Biosynthetic Pathway in Complex with Sah within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:56.1 occ:1.00 O A:HOH517 2.1 30.0 1.0 OE1 A:GLU298 2.7 24.0 1.0 OD2 A:ASP299 2.7 36.6 1.0 OD1 A:ASP270 2.8 26.6 1.0 NE2 A:HIS175 3.4 26.0 1.0 CG A:ASP270 3.4 25.2 1.0 CG A:ASP299 3.6 32.0 1.0 CD2 A:HIS175 3.6 25.4 1.0 OD2 A:ASP270 3.7 24.1 1.0 OD1 A:ASP299 3.8 37.6 1.0 CD A:GLU298 3.8 23.4 1.0 CB A:GLU298 3.9 21.8 1.0 CE2 A:PHE177 3.9 19.2 1.0 OD1 A:ASP169 4.0 33.3 1.0 CE1 A:HIS175 4.2 26.5 1.0 OD2 A:ASP169 4.4 37.5 1.0 CG A:GLU298 4.4 22.8 1.0 CG A:ASP169 4.5 32.2 1.0 CG A:HIS175 4.5 25.7 1.0 CB A:ASP270 4.6 24.9 1.0 OE2 A:GLU298 4.7 23.4 1.0 CZ A:PHE177 4.8 19.3 1.0 CD2 A:PHE177 4.8 18.6 1.0 ND1 A:HIS175 4.8 28.1 1.0 CB A:ASP299 4.8 29.7 1.0 CE1 A:HIS273 4.9 33.4 1.0 NZ A:LYS170 4.9 24.3 1.0 N A:ASP299 5.0 24.9 1.0

Magnesium binding site 2 out of 2 in the Spnk Methyltransferase From the Spinosyn Biosynthetic Pathway in Complex with Sah


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Spnk Methyltransferase From the Spinosyn Biosynthetic Pathway in Complex with Sah within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg402 b:56.1 occ:1.00 O B:HOH569 2.2 30.0 1.0 O B:HOH507 2.2 30.0 1.0 O B:HOH527 2.4 30.0 1.0 OD1 B:ASP270 2.5 24.4 1.0 OD2 B:ASP270 2.9 25.4 1.0 CG B:ASP270 3.0 25.4 1.0 OD2 B:ASP299 3.3 35.6 1.0 OD1 B:ASP169 3.3 32.3 1.0 O B:HOH619 3.6 30.0 1.0 OD2 B:ASP169 3.7 34.9 1.0 CG B:ASP169 3.9 31.6 1.0 OE1 B:GLU298 4.0 22.8 1.0 NE2 B:HIS273 4.3 32.4 1.0 CG B:ASP299 4.4 31.3 1.0 CE1 B:HIS273 4.5 32.2 1.0 NE2 B:HIS175 4.5 25.7 1.0 OXT B:SAH401 4.5 42.7 1.0 CB B:SAH401 4.5 44.6 1.0 CB B:ASP270 4.5 24.9 1.0 CD2 B:HIS175 4.7 25.2 1.0 OD1 B:ASP299 4.8 34.6 1.0 CG B:SAH401 4.8 45.1 1.0 O B:ASP270 5.0 27.9 1.0

S.Huang, H.Ji, J.Zheng. Structural and Computational Insights Into the Regioselectivity of Spnk Involved in Rhamnose Methylation of Spinosyn. Int.J.Biol.Macromol. V. 253 26763 2023.
ISSN: ISSN 0141-8130
PubMed: 37703985
DOI: 10.1016/J.IJBIOMAC.2023.126763