Magnesium in PDB 8rwm: Crystal Structure of Selenomethionine Derivatized Alpha Keto Acid C- Methyl-Transferases Mrsa

The structure of Crystal Structure of Selenomethionine Derivatized Alpha Keto Acid C- Methyl-Transferases Mrsa, PDB code: 8rwm was solved by S.Gerhardt, J.N.Andexer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	74.82 / 1.64
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	147.847, 65.531, 74.823, 90, 90, 90
R / Rfree (%)	16 / 18.3

The structure of Crystal Structure of Selenomethionine Derivatized Alpha Keto Acid C- Methyl-Transferases Mrsa also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Magnesium atom in the Crystal Structure of Selenomethionine Derivatized Alpha Keto Acid C- Methyl-Transferases Mrsa (pdb code 8rwm). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of Selenomethionine Derivatized Alpha Keto Acid C- Methyl-Transferases Mrsa, PDB code: 8rwm:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Crystal Structure of Selenomethionine Derivatized Alpha Keto Acid C- Methyl-Transferases Mrsa


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Selenomethionine Derivatized Alpha Keto Acid C- Methyl-Transferases Mrsa within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1001 b:16.5 occ:1.00 NE2 A:HIS264 2.0 22.2 1.0 OE1 A:GLN327 2.1 34.6 1.0 O A:HOH1112 2.1 32.1 1.0 NE2 A:HIS322 2.3 23.5 1.0 O A:HOH1122 2.3 41.0 1.0 CD2 A:HIS264 3.0 21.4 1.0 CE1 A:HIS264 3.0 24.0 1.0 CD A:GLN327 3.1 33.6 1.0 O A:HOH1213 3.2 29.8 1.0 CE1 A:HIS322 3.2 23.6 1.0 HD2 A:HIS264 3.2 21.4 1.0 HE22 A:GLN327 3.2 35.4 1.0 HE1 A:HIS264 3.3 23.9 1.0 HE1 A:HIS322 3.3 23.6 1.0 CD2 A:HIS322 3.3 22.2 1.0 NE2 A:GLN327 3.6 35.4 1.0 HD2 A:HIS322 3.6 22.2 1.0 OH A:TYR318 3.8 27.0 1.0 HG2 A:GLU265 4.0 30.8 1.0 HG3 A:GLU265 4.0 30.8 1.0 HB3 A:GLN327 4.0 24.4 1.0 HB3 A:PHE261 4.1 17.2 1.0 CG A:HIS264 4.1 20.2 1.0 ND1 A:HIS264 4.2 23.1 1.0 HH A:TYR318 4.2 27.0 1.0 HH A:TYR131 4.2 22.9 1.0 HD21 A:LEU329 4.3 17.3 1.0 ND1 A:HIS322 4.4 23.1 1.0 CG A:GLN327 4.4 27.2 1.0 CG A:HIS322 4.4 21.4 1.0 CZ A:TYR318 4.5 23.2 1.0 CG A:GLU265 4.5 30.8 1.0 OE2 A:GLU265 4.5 43.3 1.0 HE21 A:GLN327 4.6 35.4 1.0 HH12 A:ARG151 4.6 32.1 1.0 O A:PHE261 4.6 22.3 1.0 HE1 A:TYR318 4.6 23.2 1.0 HG2 A:GLN327 4.6 27.2 1.0 CB A:GLN327 4.6 24.4 1.0 OH A:TYR131 4.8 22.9 1.0 HB2 A:GLN327 4.8 24.4 1.0 CE1 A:TYR318 4.8 23.2 1.0 HD11 A:LEU321 4.9 28.1 1.0 O A:HOH1493 5.0 72.9 1.0

Magnesium binding site 2 out of 3 in the Crystal Structure of Selenomethionine Derivatized Alpha Keto Acid C- Methyl-Transferases Mrsa


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Selenomethionine Derivatized Alpha Keto Acid C- Methyl-Transferases Mrsa within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1002 b:32.0 occ:1.00 O A:GLN327 2.3 23.2 1.0 O A:THR325 2.4 20.2 1.0 O A:HOH1511 2.5 48.7 1.0 O A:HIS322 2.6 25.1 1.0 H A:GLN327 2.6 21.0 1.0 O A:HOH1376 3.1 35.8 1.0 N A:GLN327 3.4 20.9 1.0 C A:GLN327 3.4 21.0 1.0 HA A:CYS323 3.5 18.5 1.0 HA A:ASN326 3.5 19.7 1.0 C A:THR325 3.6 19.2 1.0 HZ3 A:TRP148 3.6 26.9 1.0 C A:HIS322 3.7 20.8 1.0 CZ3 A:TRP148 3.8 26.9 1.0 HH2 A:TRP148 3.9 27.9 1.0 HA A:LEU328 4.0 18.9 1.0 CH2 A:TRP148 4.0 27.9 1.0 H A:THR325 4.0 18.1 1.0 CA A:GLN327 4.1 21.4 1.0 C A:CYS323 4.1 18.7 1.0 CA A:CYS323 4.1 18.5 1.0 CA A:ASN326 4.2 19.8 1.0 C A:ASN326 4.2 21.5 1.0 HD13 A:LEU328 4.2 27.2 1.0 HB2 A:GLN327 4.3 24.4 1.0 N A:CYS323 4.3 18.1 1.0 O A:CYS323 4.3 20.8 1.0 N A:ASN326 4.4 18.7 1.0 O A:HOH1146 4.4 27.9 1.0 N A:THR325 4.4 18.0 1.0 N A:LEU328 4.5 18.8 1.0 HB2 A:LEU328 4.5 21.4 1.0 CE3 A:TRP148 4.5 25.8 1.0 HA A:HIS322 4.5 18.4 1.0 O A:HOH1379 4.6 18.4 1.0 N A:PHE324 4.6 17.4 1.0 CA A:THR325 4.7 18.2 1.0 CA A:LEU328 4.7 18.9 1.0 HB3 A:HIS322 4.7 19.4 1.0 CA A:HIS322 4.8 18.4 1.0 CZ2 A:TRP148 4.8 27.7 1.0 CB A:GLN327 4.8 24.4 1.0 HD12 A:LEU328 4.9 27.2 1.0 HE3 A:TRP148 4.9 25.8 1.0 H A:PHE324 4.9 17.4 1.0 HA A:GLN327 4.9 21.4 1.0

Magnesium binding site 3 out of 3 in the Crystal Structure of Selenomethionine Derivatized Alpha Keto Acid C- Methyl-Transferases Mrsa


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Selenomethionine Derivatized Alpha Keto Acid C- Methyl-Transferases Mrsa within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg401 b:17.3 occ:1.00 NE2 B:HIS264 1.9 25.2 1.0 O B:HOH546 2.0 40.0 1.0 NE2 B:GLN327 2.0 29.7 1.0 O B:HOH666 2.3 37.8 1.0 NE2 B:HIS322 2.3 25.4 1.0 HE21 B:GLN327 2.4 29.7 1.0 CD2 B:HIS264 2.9 23.9 1.0 CE1 B:HIS264 2.9 25.1 1.0 CD B:GLN327 3.1 32.5 1.0 HD2 B:HIS264 3.2 23.9 1.0 HE1 B:HIS264 3.2 25.1 1.0 CE1 B:HIS322 3.2 25.2 1.0 HE1 B:HIS322 3.3 25.2 1.0 CD2 B:HIS322 3.4 23.6 1.0 OE1 B:GLN327 3.5 36.7 1.0 O B:HOH553 3.6 29.5 1.0 HD2 B:HIS322 3.7 23.6 1.0 OH B:TYR318 3.8 25.8 1.0 HG3 B:GLU265 3.9 33.4 1.0 HH B:TYR318 3.9 25.8 1.0 CG B:HIS264 4.0 22.0 1.0 ND1 B:HIS264 4.1 23.9 1.0 HB3 B:PHE261 4.1 21.1 1.0 HB3 B:GLN327 4.1 26.7 1.0 HG2 B:GLU265 4.2 33.4 1.0 HD21 B:LEU329 4.3 17.5 1.0 ND1 B:HIS322 4.4 23.9 1.0 CG B:GLN327 4.4 29.4 1.0 CZ B:TYR318 4.4 23.3 1.0 CG B:HIS322 4.5 21.9 1.0 CG B:GLU265 4.5 33.4 1.0 O B:PHE261 4.6 25.5 1.0 OE2 B:GLU265 4.6 47.1 1.0 HG2 B:GLN327 4.6 29.4 1.0 HH B:TYR131 4.6 21.3 1.0 HE1 B:TYR318 4.6 22.5 1.0 CB B:GLN327 4.7 26.6 1.0 HH12 B:ARG151 4.7 33.0 1.0 O B:HOH703 4.8 64.7 1.0 HB2 B:GLN327 4.8 26.6 1.0 CE1 B:TYR318 4.8 22.5 1.0 HD23 B:LEU329 4.9 17.5 1.0 O B:HOH526 4.9 70.3 1.0 OH B:TYR131 5.0 21.3 1.0 HD1 B:HIS264 5.0 23.9 1.0

C.Sommer-Kamann, J.Breiltgens, Z.Zou, S.Gerhardt, R.Saleem-Batcha, F.Kemper, O.Einsle, J.N.Andexer, M.Muller. Structures and Protein Engineering of the Alpha-Keto Acid C-Methyltransferases Sgvm and Mrsa For Rational Substrate Transfer. Chembiochem 00258 2024.
ISSN: ESSN 1439-7633
PubMed: 38887142
DOI: 10.1002/CBIC.202400258