Magnesium in PDB 4x7x: Mycf Mycinamicin III 3'-O-Methyltransferase (E35Q, E139A Variant) in Complex with Mg, Sah and Macrocin

All present enzymatic activity of Mycf Mycinamicin III 3'-O-Methyltransferase (E35Q, E139A Variant) in Complex with Mg, Sah and Macrocin:
2.1.1.237;

The structure of Mycf Mycinamicin III 3'-O-Methyltransferase (E35Q, E139A Variant) in Complex with Mg, Sah and Macrocin, PDB code: 4x7x was solved by S.M.Bernard, J.L.Smith, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.05 / 1.75
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	50.229, 91.642, 128.427, 90.00, 90.00, 90.00
R / Rfree (%)	16.5 / 18.6

The binding sites of Magnesium atom in the Mycf Mycinamicin III 3'-O-Methyltransferase (E35Q, E139A Variant) in Complex with Mg, Sah and Macrocin (pdb code 4x7x). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Mycf Mycinamicin III 3'-O-Methyltransferase (E35Q, E139A Variant) in Complex with Mg, Sah and Macrocin, PDB code: 4x7x:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Mycf Mycinamicin III 3'-O-Methyltransferase (E35Q, E139A Variant) in Complex with Mg, Sah and Macrocin


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Mycf Mycinamicin III 3'-O-Methyltransferase (E35Q, E139A Variant) in Complex with Mg, Sah and Macrocin within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:11.7 occ:1.00 O15 A:3ZP303 2.1 22.2 1.0 OD1 A:ASP217 2.1 18.2 1.0 OD1 A:ASP189 2.2 15.8 1.0 OD2 A:ASP216 2.2 16.3 1.0 O A:HOH458 2.3 14.0 1.0 O14 A:3ZP303 2.4 19.1 1.0 O A:HOH523 2.6 21.4 1.0 C40 A:3ZP303 3.0 21.5 1.0 CG A:ASP217 3.1 16.4 1.0 C41 A:3ZP303 3.2 20.2 1.0 CG A:ASP216 3.3 14.8 1.0 CG A:ASP189 3.3 15.5 1.0 OD2 A:ASP217 3.4 17.0 1.0 OD2 A:ASP191 3.7 22.3 1.0 OD2 A:ASP189 3.7 16.3 1.0 C42 A:3ZP303 3.8 19.7 1.0 CB A:ASP216 3.9 14.1 1.0 O A:HOH462 4.2 13.8 1.0 OD1 A:ASP216 4.2 15.8 1.0 OD1 A:ASP191 4.3 22.6 1.0 CG A:ASP191 4.3 20.7 1.0 C39 A:3ZP303 4.4 24.0 1.0 CB A:ASP217 4.4 15.4 1.0 CB A:ASP189 4.6 14.7 1.0 C A:ASP216 4.6 14.2 1.0 NH2 A:ARG61 4.6 13.2 1.0 C43 A:3ZP303 4.7 19.2 1.0 N A:ASP217 4.7 14.3 1.0 O A:ASP216 4.7 15.0 1.0 OE1 A:GLN246 4.7 15.5 1.0 CA A:ASP217 4.7 14.7 1.0 O A:ASP189 4.8 15.6 1.0 CA A:ASP189 4.8 14.5 1.0 O16 A:3ZP303 4.8 27.4 1.0 C A:ASP189 4.9 14.9 1.0 CA A:ASP216 4.9 13.9 1.0 C38 A:3ZP303 5.0 23.4 1.0 O13 A:3ZP303 5.0 20.4 1.0

Magnesium binding site 2 out of 2 in the Mycf Mycinamicin III 3'-O-Methyltransferase (E35Q, E139A Variant) in Complex with Mg, Sah and Macrocin


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Mycf Mycinamicin III 3'-O-Methyltransferase (E35Q, E139A Variant) in Complex with Mg, Sah and Macrocin within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg302 b:10.9 occ:1.00 OD1 B:ASP217 2.0 17.7 1.0 OD2 B:ASP216 2.2 14.9 1.0 O15 B:3ZP303 2.2 20.5 1.0 OD1 B:ASP189 2.2 15.5 1.0 O B:HOH524 2.3 14.9 1.0 O14 B:3ZP303 2.4 18.8 1.0 O B:HOH523 2.6 21.2 1.0 CG B:ASP217 3.0 15.9 1.0 C40 B:3ZP303 3.1 20.9 1.0 C41 B:3ZP303 3.2 19.7 1.0 CG B:ASP189 3.2 15.0 1.0 CG B:ASP216 3.2 13.8 1.0 OD2 B:ASP217 3.4 16.5 1.0 OD2 B:ASP189 3.6 15.2 1.0 OD2 B:ASP191 3.7 22.1 1.0 C42 B:3ZP303 3.9 20.3 1.0 CB B:ASP216 3.9 13.1 1.0 O B:HOH525 4.2 15.3 1.0 OD1 B:ASP216 4.2 15.0 1.0 CB B:ASP217 4.4 14.6 1.0 CG B:ASP191 4.4 20.4 1.0 OD1 B:ASP191 4.4 21.5 1.0 C39 B:3ZP303 4.5 23.4 1.0 CB B:ASP189 4.6 14.4 1.0 C B:ASP216 4.6 13.1 1.0 NH2 B:ARG61 4.6 14.6 1.0 O B:ASP189 4.7 15.5 1.0 N B:ASP217 4.7 13.1 1.0 C43 B:3ZP303 4.7 19.5 1.0 O B:ASP216 4.7 13.2 1.0 CA B:ASP217 4.7 13.8 1.0 CA B:ASP189 4.8 14.3 1.0 OE1 B:GLN246 4.8 16.8 1.0 C B:ASP189 4.9 14.8 1.0 O16 B:3ZP303 4.9 26.8 1.0 CA B:ASP216 4.9 12.7 1.0

S.M.Bernard, D.L.Akey, A.Tripathi, S.R.Park, J.R.Konwerski, Y.Anzai, S.Li, F.Kato, D.H.Sherman, J.L.Smith. Structural Basis of Substrate Specificity and Regiochemistry in the Mycf/Tylf Family of Sugar O-Methyltransferases. Acs Chem.Biol. 2015.
ISSN: ESSN 1554-8937
PubMed: 25692963
DOI: 10.1021/CB5009348