Sodium 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:

Magnesium

(Mg)

3 atoms

The binding sites of Sodium 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 Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of Selenomethionine Derivatized Alpha Keto Acid C- Methyl-Transferases Mrsa, PDB code: 8rwm:

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


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na 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 B:Na402 b:33.9 occ:1.00 O B:THR325 2.3 20.0 1.0 O B:GLN327 2.4 26.0 1.0 O B:HIS322 2.5 22.9 1.0 H B:GLN327 2.6 23.8 1.0 O B:HOH880 2.9 41.1 1.0 O B:HOH733 3.1 34.1 1.0 N B:GLN327 3.4 23.8 1.0 HA B:ASN326 3.4 20.6 1.0 C B:GLN327 3.5 24.6 1.0 HA B:CYS323 3.5 18.0 1.0 C B:THR325 3.5 18.8 1.0 HZ3 B:TRP148 3.6 25.1 1.0 C B:HIS322 3.6 20.2 1.0 CZ3 B:TRP148 3.8 25.1 1.0 HH2 B:TRP148 3.9 25.3 1.0 H B:THR325 3.9 17.5 1.0 CH2 B:TRP148 4.0 25.3 1.0 HA B:LEU328 4.1 21.1 1.0 C B:CYS323 4.1 18.8 1.0 CA B:GLN327 4.1 24.5 1.0 CA B:CYS323 4.1 17.9 1.0 CA B:ASN326 4.2 20.6 1.0 C B:ASN326 4.2 23.0 1.0 O B:HOH537 4.3 28.2 1.0 HB2 B:GLN327 4.3 26.6 1.0 N B:ASN326 4.3 19.0 1.0 O B:CYS323 4.3 20.2 1.0 N B:CYS323 4.3 17.6 1.0 N B:THR325 4.3 17.4 1.0 HD13 B:LEU328 4.4 29.7 1.0 HA B:HIS322 4.5 18.7 1.0 N B:LEU328 4.5 21.8 1.0 CE3 B:TRP148 4.5 23.8 1.0 HB2 B:LEU328 4.6 23.2 1.0 N B:PHE324 4.6 17.9 1.0 CA B:THR325 4.6 16.8 1.0 O B:HOH742 4.6 19.4 1.0 CA B:HIS322 4.7 18.7 1.0 CA B:LEU328 4.8 21.1 1.0 HB3 B:HIS322 4.8 19.7 1.0 CB B:GLN327 4.8 26.6 1.0 CZ2 B:TRP148 4.8 25.1 1.0 HE3 B:TRP148 4.8 23.8 1.0 H B:PHE324 4.9 17.9 1.0 OG1 B:THR325 4.9 20.0 1.0 HD12 B:LEU328 4.9 29.7 1.0 HG1 B:THR325 5.0 20.0 1.0 HA B:GLN327 5.0 24.5 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