Manganese in PDB 7ucl: Sxta Methyltransferase Variant F458H in Complex with MN2+ and Malonate

The structure of Sxta Methyltransferase Variant F458H in Complex with MN2+ and Malonate, PDB code: 7ucl was solved by Y.Lao, J.L.Smith, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.34 / 2.09
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	78.64, 83.794, 117.821, 90, 103.09, 90
R / Rfree (%)	20.6 / 23.9

The binding sites of Manganese atom in the Sxta Methyltransferase Variant F458H in Complex with MN2+ and Malonate (pdb code 7ucl). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Sxta Methyltransferase Variant F458H in Complex with MN2+ and Malonate, PDB code: 7ucl:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Sxta Methyltransferase Variant F458H in Complex with MN2+ and Malonate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Sxta Methyltransferase Variant F458H in Complex with MN2+ and Malonate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn802 b:35.5 occ:1.00 O8 A:MLI801 1.9 39.2 1.0 O A:HOH956 2.1 39.7 1.0 O6 A:MLI801 2.1 37.7 1.0 OE1 A:GLN464 2.2 38.0 1.0 NE2 A:HIS372 2.3 34.7 1.0 OE1 A:GLN459 2.3 36.6 1.0 C3 A:MLI801 2.9 43.3 1.0 C2 A:MLI801 3.1 39.0 1.0 CD2 A:HIS372 3.1 37.1 1.0 CD A:GLN464 3.2 38.5 1.0 CD A:GLN459 3.3 34.1 1.0 CE1 A:HIS372 3.3 36.5 1.0 C1 A:MLI801 3.4 43.5 1.0 NE2 A:GLN459 3.6 33.8 1.0 NE2 A:GLN464 3.7 32.9 1.0 O9 A:MLI801 4.1 50.5 1.0 O7 A:MLI801 4.2 38.6 1.0 CG A:HIS372 4.3 36.1 1.0 OD2 A:ASP373 4.3 45.0 1.0 ND1 A:HIS372 4.4 38.0 1.0 CB A:ASP373 4.5 40.1 1.0 CG A:GLN464 4.5 33.1 1.0 CG A:ASP373 4.5 42.6 1.0 CG A:GLN459 4.7 30.5 1.0 CB A:GLN464 4.7 36.0 1.0 CZ A:PHE455 4.9 37.0 1.0

Manganese binding site 2 out of 2 in the Sxta Methyltransferase Variant F458H in Complex with MN2+ and Malonate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Sxta Methyltransferase Variant F458H in Complex with MN2+ and Malonate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn802 b:36.8 occ:1.00 O8 B:MLI801 1.8 40.0 1.0 OE1 B:GLN464 2.0 40.6 1.0 O B:HOH933 2.0 42.8 1.0 OE1 B:GLN459 2.3 40.1 1.0 O6 B:MLI801 2.3 38.3 1.0 NE2 B:HIS372 2.3 36.8 1.0 C3 B:MLI801 2.9 47.5 1.0 CD B:GLN464 2.9 41.6 1.0 C2 B:MLI801 3.1 44.5 1.0 CD2 B:HIS372 3.2 41.3 1.0 CD B:GLN459 3.2 38.3 1.0 NE2 B:GLN464 3.4 37.3 1.0 CE1 B:HIS372 3.4 42.7 1.0 C1 B:MLI801 3.4 45.2 1.0 NE2 B:GLN459 3.5 41.9 1.0 O9 B:MLI801 4.0 52.3 1.0 CG B:GLN464 4.2 40.0 1.0 OD2 B:ASP373 4.3 46.4 1.0 O7 B:MLI801 4.3 46.7 1.0 CG B:HIS372 4.4 38.0 1.0 ND1 B:HIS372 4.4 36.4 1.0 CG B:ASP373 4.6 45.0 1.0 CG B:GLN459 4.6 36.2 1.0 CB B:ASP373 4.6 38.8 1.0 CB B:GLN464 4.6 39.8 1.0 CZ B:PHE455 4.8 40.4 1.0

Y.Lao, M.A.Skiba, S.W.Chun, A.R.H.Narayan, J.L.Smith. Structural Basis For Control of Methylation Extent in Polyketide Synthase Metal-Dependent C -Methyltransferases. Acs Chem.Biol. V. 17 2088 2022.
ISSN: ESSN 1554-8937
PubMed: 35594521
DOI: 10.1021/ACSCHEMBIO.2C00085