Manganese in PDB 7uci: Sxta Methyltransferase and Decarboxylase Didomain in Complex with MN2+ and Sah

The structure of Sxta Methyltransferase and Decarboxylase Didomain in Complex with MN2+ and Sah, PDB code: 7uci was solved by Y.Lao, M.A.Skiba, J.L.Smith, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.43 / 2.60
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	43.802, 69.668, 127.608, 86.44, 83.26, 83.95
R / Rfree (%)	23.8 / 29.8

The binding sites of Manganese atom in the Sxta Methyltransferase and Decarboxylase Didomain in Complex with MN2+ and Sah (pdb code 7uci). 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 and Decarboxylase Didomain in Complex with MN2+ and Sah, PDB code: 7uci:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Sxta Methyltransferase and Decarboxylase Didomain in Complex with MN2+ and Sah


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Sxta Methyltransferase and Decarboxylase Didomain in Complex with MN2+ and Sah within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn802 b:48.0 occ:1.00 OE1 A:GLN464 2.0 47.0 1.0 O A:HOH937 2.0 30.0 1.0 OE1 A:GLN459 2.5 53.0 1.0 HE22 A:GLN464 2.6 82.8 1.0 O A:HOH938 2.6 26.1 1.0 NE2 A:HIS372 2.6 52.8 1.0 O A:HOH944 2.7 35.0 1.0 HE22 A:GLN459 2.8 59.7 1.0 CD A:GLN464 2.8 47.3 1.0 NE2 A:GLN464 3.0 69.0 1.0 CD A:GLN459 3.3 51.9 1.0 NE2 A:GLN459 3.3 49.7 1.0 HD2 A:HIS372 3.3 51.6 1.0 CD2 A:HIS372 3.4 43.0 1.0 CE1 A:HIS372 3.7 49.7 1.0 HE21 A:GLN464 3.9 82.8 1.0 HE1 A:HIS372 3.9 59.6 1.0 HB2 A:ASP373 4.0 63.0 1.0 HE21 A:GLN459 4.1 59.7 1.0 HZ A:PHE455 4.2 36.6 1.0 OD2 A:ASP373 4.2 58.8 1.0 CG A:GLN464 4.3 41.2 1.0 HB3 A:GLN464 4.4 66.0 1.0 CG A:HIS372 4.6 41.8 1.0 ND1 A:HIS372 4.7 45.7 1.0 CG A:GLN459 4.7 45.8 1.0 HG2 A:GLN464 4.7 49.5 1.0 O A:PHE369 4.7 51.6 1.0 CB A:GLN464 4.7 55.0 1.0 HB2 A:GLN464 4.8 66.0 1.0 HG3 A:GLN464 4.8 49.5 1.0 HB3 A:GLN459 4.8 35.1 1.0 CZ A:PHE455 4.8 30.5 1.0 CB A:ASP373 4.9 52.5 1.0 CG A:ASP373 4.9 51.4 1.0

Manganese binding site 2 out of 2 in the Sxta Methyltransferase and Decarboxylase Didomain in Complex with MN2+ and Sah


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Sxta Methyltransferase and Decarboxylase Didomain in Complex with MN2+ and Sah within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn802 b:56.7 occ:1.00 O B:HOH938 2.0 71.7 1.0 NE2 B:HIS372 2.1 70.5 1.0 O B:HOH928 2.2 39.2 1.0 OE1 B:GLN464 2.2 74.1 1.0 O B:HOH930 2.4 57.7 1.0 CD2 B:HIS372 2.9 55.9 1.0 HD2 B:HIS372 3.0 67.0 1.0 HE22 B:GLN464 3.0 97.3 1.0 CD B:GLN464 3.0 71.2 1.0 OE1 B:GLN459 3.1 57.0 1.0 CE1 B:HIS372 3.2 47.1 1.0 NE2 B:GLN464 3.4 81.1 1.0 HE1 B:HIS372 3.5 56.5 1.0 HB2 B:ASP373 3.6 79.1 1.0 HE22 B:GLN459 4.0 69.1 1.0 CD B:GLN459 4.1 55.6 1.0 CG B:HIS372 4.2 43.4 1.0 HE21 B:GLN464 4.2 97.3 1.0 HB3 B:GLN464 4.2 72.4 1.0 ND1 B:HIS372 4.3 45.5 1.0 OD2 B:ASP373 4.3 78.5 1.0 CG B:GLN464 4.4 49.6 1.0 NE2 B:GLN459 4.4 57.6 1.0 CB B:ASP373 4.5 65.9 1.0 O B:PHE369 4.6 74.3 1.0 CB B:GLN464 4.7 60.4 1.0 HG2 B:GLN464 4.7 59.5 1.0 HB2 B:GLN464 4.7 72.4 1.0 CG B:ASP373 4.7 68.2 1.0 HZ B:PHE455 4.8 51.4 1.0 HB3 B:PHE369 4.9 72.2 1.0 HB3 B:ASP373 4.9 79.1 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