Magnesium in PDB 4x7u: Mycf Mycinamicin III 3'-O-Methyltransferase in Complex with Mg, Sah and Mycinamicin III (Substrate)

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

The structure of Mycf Mycinamicin III 3'-O-Methyltransferase in Complex with Mg, Sah and Mycinamicin III (Substrate), PDB code: 4x7u 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)	43.71 / 1.65
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	49.856, 90.850, 128.641, 90.00, 90.00, 90.00
R / Rfree (%)	14.8 / 16.8

The binding sites of Magnesium atom in the Mycf Mycinamicin III 3'-O-Methyltransferase in Complex with Mg, Sah and Mycinamicin III (Substrate) (pdb code 4x7u). 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 in Complex with Mg, Sah and Mycinamicin III (Substrate), PDB code: 4x7u:
Jump to Magnesium binding site number: 1; 2;

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


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 in Complex with Mg, Sah and Mycinamicin III (Substrate) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:8.6 occ:1.00 OD1 A:ASP217 2.1 17.4 1.0 OD2 A:ASP216 2.2 14.2 1.0 OD1 A:ASP189 2.3 14.5 1.0 O A:HOH522 2.4 16.3 1.0 O10 A:ZM3303 2.4 17.4 1.0 O9 A:ZM3303 2.4 19.7 1.0 O A:HOH545 2.5 17.9 1.0 CG A:ASP217 3.1 15.9 1.0 CG A:ASP216 3.3 13.5 1.0 C35 A:ZM3303 3.3 18.9 1.0 C33 A:ZM3303 3.4 19.6 1.0 CG A:ASP189 3.4 13.9 1.0 OD2 A:ASP217 3.5 16.6 1.0 OD2 A:ASP189 3.8 14.0 1.0 C36 A:ZM3303 3.9 19.4 1.0 CB A:ASP216 4.0 13.0 1.0 OD2 A:ASP191 4.0 18.4 1.0 OD1 A:ASP216 4.1 13.6 1.0 O A:HOH525 4.1 15.3 1.0 OD1 A:ASP191 4.2 19.1 1.0 CG A:ASP191 4.4 17.9 1.0 CB A:ASP217 4.4 15.1 1.0 C37 A:ZM3303 4.6 18.8 1.0 CB A:ASP189 4.7 13.5 1.0 C A:ASP216 4.7 13.2 1.0 O A:ASP189 4.7 14.4 1.0 NH2 A:ARG61 4.7 12.3 1.0 C31 A:ZM3303 4.7 21.1 1.0 N A:ASP217 4.7 13.8 1.0 OE1 A:GLN246 4.8 16.1 1.0 CA A:ASP217 4.8 14.2 1.0 CA A:ASP189 4.8 13.3 1.0 O A:ASP216 4.8 14.0 1.0 C A:ASP189 4.9 14.0 1.0

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


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 in Complex with Mg, Sah and Mycinamicin III (Substrate) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg301 b:10.2 occ:1.00 OD1 B:ASP217 2.2 15.7 1.0 OD1 B:ASP189 2.2 13.9 1.0 OD1 B:ASP216 2.2 15.2 1.0 O9 B:ZM3303 2.3 22.6 1.0 O B:HOH547 2.4 18.0 1.0 O10 B:ZM3303 2.4 20.7 1.0 O B:HOH566 2.5 20.7 1.0 C33 B:ZM3303 3.2 23.6 1.0 CG B:ASP217 3.2 14.5 1.0 C35 B:ZM3303 3.2 21.9 1.0 CG B:ASP216 3.3 14.3 1.0 CG B:ASP189 3.3 13.5 1.0 OD2 B:ASP217 3.5 14.4 1.0 OD2 B:ASP189 3.7 13.6 1.0 C36 B:ZM3303 3.8 22.8 1.0 CB B:ASP216 4.0 13.2 1.0 OD2 B:ASP191 4.0 18.0 1.0 O B:HOH516 4.1 15.4 1.0 OD2 B:ASP216 4.2 14.6 1.0 OD1 B:ASP191 4.3 17.4 1.0 CG B:ASP191 4.5 16.4 1.0 CB B:ASP217 4.5 13.9 1.0 C31 B:ZM3303 4.5 24.8 1.0 CB B:ASP189 4.6 13.1 1.0 C37 B:ZM3303 4.6 22.1 1.0 NH2 B:ARG61 4.6 12.5 1.0 C B:ASP216 4.7 13.5 1.0 O B:ASP189 4.7 13.9 1.0 O B:ASP216 4.8 14.1 1.0 N B:ASP217 4.8 13.4 1.0 CA B:ASP189 4.8 12.8 1.0 CA B:ASP217 4.8 13.5 1.0 C B:ASP189 4.9 13.2 1.0 O8 B:ZM3303 4.9 28.2 1.0 OE1 B:GLN246 4.9 18.0 1.0 C30 B:ZM3303 5.0 24.9 1.0 O11 B:ZM3303 5.0 23.8 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