Manganese in PDB 7uch: Apra Methyltransferase 1 - Gnat in Complex with MN2+ , Sam, and Di- Methyl-Malonate

The structure of Apra Methyltransferase 1 - Gnat in Complex with MN2+ , Sam, and Di- Methyl-Malonate, PDB code: 7uch was solved by M.A.Skiba, Y.Lao, J.L.Smith, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.23 / 2.18
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	60.572, 88.283, 135.982, 90, 90, 90
R / Rfree (%)	19.3 / 24.1

The binding sites of Manganese atom in the Apra Methyltransferase 1 - Gnat in Complex with MN2+ , Sam, and Di- Methyl-Malonate (pdb code 7uch). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Apra Methyltransferase 1 - Gnat in Complex with MN2+ , Sam, and Di- Methyl-Malonate, PDB code: 7uch:

Manganese binding site 1 out of 1 in the Apra Methyltransferase 1 - Gnat in Complex with MN2+ , Sam, and Di- Methyl-Malonate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Apra Methyltransferase 1 - Gnat in Complex with MN2+ , Sam, and Di- Methyl-Malonate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn801 b:30.5 occ:1.00 OAF A:MU6803 2.0 28.2 1.0 OE1 A:GLN461 2.1 27.5 1.0 O A:HOH930 2.2 23.3 1.0 OAE A:MU6803 2.3 35.5 1.0 NE2 A:HIS456 2.3 30.0 1.0 NE2 A:HIS369 2.4 25.0 1.0 CAB A:MU6803 3.0 32.9 1.0 CD A:GLN461 3.1 27.2 1.0 CD2 A:HIS456 3.1 25.6 1.0 CD2 A:HIS369 3.2 25.0 1.0 CE1 A:HIS456 3.3 32.2 1.0 CAD A:MU6803 3.3 37.2 1.0 CE1 A:HIS369 3.4 26.4 1.0 NE2 A:GLN461 3.5 28.9 1.0 CAC A:MU6803 3.7 45.6 1.0 OAA A:MU6803 4.0 33.3 1.0 O A:HOH1049 4.0 31.2 1.0 OD2 A:ASP370 4.1 37.4 1.0 CG A:HIS456 4.3 29.9 1.0 CAH A:MU6803 4.3 26.9 1.0 ND1 A:HIS456 4.3 31.5 1.0 OAG A:MU6803 4.4 36.4 1.0 CG A:HIS369 4.4 24.4 1.0 CG A:GLN461 4.5 23.4 1.0 ND1 A:HIS369 4.5 28.1 1.0 CG A:ASP370 4.6 40.9 1.0 O A:HOH939 4.7 50.3 1.0 CB A:ASP370 4.8 32.2 1.0 CB A:GLN461 4.9 29.1 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