Sodium in PDB 7mcl: Crystal Structure of Staphylococcus Aureus Cystathionine Gamma-Lyase, Plp Bound

All present enzymatic activity of Crystal Structure of Staphylococcus Aureus Cystathionine Gamma-Lyase, Plp Bound:
2.5.1.48; 4.4.1.1; 4.4.1.8;

The structure of Crystal Structure of Staphylococcus Aureus Cystathionine Gamma-Lyase, Plp Bound, PDB code: 7mcl was solved by A.Nuthanakanti, A.Serganov, A.Kaushik, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.96 / 2.40
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	104.966, 104.966, 289.569, 90, 90, 90
R / Rfree (%)	18.1 / 21.4

The binding sites of Sodium atom in the Crystal Structure of Staphylococcus Aureus Cystathionine Gamma-Lyase, Plp Bound (pdb code 7mcl). 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 Staphylococcus Aureus Cystathionine Gamma-Lyase, Plp Bound, PDB code: 7mcl:

Sodium binding site 1 out of 1 in the Crystal Structure of Staphylococcus Aureus Cystathionine Gamma-Lyase, Plp Bound


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 Staphylococcus Aureus Cystathionine Gamma-Lyase, Plp Bound within 5.0Å range: probe atom residue distance (Å) B Occ H:Na404 b:66.5 occ:1.00 O H:HOH510 2.8 43.0 1.0 O H:HOH646 3.2 58.0 1.0 NZ H:LYS162 3.7 59.0 1.0 O H:GLY186 3.9 46.0 1.0 CE H:LYS162 4.4 52.5 1.0 C H:GLY186 4.4 37.9 1.0 OD1 H:ASP188 4.4 44.5 1.0 O H:ILE187 4.4 40.3 1.0 O H:HOH564 4.5 41.2 1.0 CA H:GLY186 4.5 33.6 1.0 O H:HOH560 4.6 46.4 1.0

K.Shatalin, A.Nuthanakanti, A.Kaushik, D.Shishov, A.Peselis, I.Shamovsky, B.Pani, M.Lechpammer, N.Vasilyev, E.Shatalina, D.Rebatchouk, A.Mironov, P.Fedichev, A.Serganov, E.Nudler. Inhibitors of Bacterial H 2 S Biogenesis Targeting Antibiotic Resistance and Tolerance. Science V. 372 1169 2021.
ISSN: ESSN 1095-9203
PubMed: 34112687
DOI: 10.1126/SCIENCE.ABD8377