Sodium in PDB 1es3: C98A Mutant of Streptomyces K15 Dd-Transpeptidase

All present enzymatic activity of C98A Mutant of Streptomyces K15 Dd-Transpeptidase:
3.4.16.4;

The structure of C98A Mutant of Streptomyces K15 Dd-Transpeptidase, PDB code: 1es3 was solved by E.Fonze, P.Charlier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.305, 54.090, 108.769, 90.00, 90.00, 90.00
R / Rfree (%)	17.4 / 24.5

The binding sites of Sodium atom in the C98A Mutant of Streptomyces K15 Dd-Transpeptidase (pdb code 1es3). 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 C98A Mutant of Streptomyces K15 Dd-Transpeptidase, PDB code: 1es3:

Sodium binding site 1 out of 1 in the C98A Mutant of Streptomyces K15 Dd-Transpeptidase


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of C98A Mutant of Streptomyces K15 Dd-Transpeptidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Na600 b:6.3 occ:1.00 O A:HOH336 3.1 42.1 1.0 OG1 A:THR214 3.3 11.6 1.0 OG A:SER216 3.7 14.3 1.0 NH2 A:ARG248 3.7 16.7 1.0 O A:HOH403 3.8 36.5 1.0 CB A:THR214 3.9 9.8 1.0 N A:GLY215 4.0 11.3 1.0 CA A:GLY215 4.2 10.3 1.0 C A:THR214 4.2 10.3 1.0 C A:GLY215 4.2 11.2 1.0 OG A:SER35 4.3 17.6 1.0 NH1 A:ARG248 4.4 15.4 1.0 N A:SER216 4.4 14.1 1.0 CB A:SER216 4.5 12.7 1.0 CZ A:ARG248 4.5 17.2 1.0 O A:THR214 4.6 12.2 1.0 OG1 A:THR199 4.7 15.8 1.0 O A:GLY215 4.7 13.3 1.0 OG A:SER96 4.7 8.0 1.0 CB A:THR199 4.7 14.1 1.0 CG2 A:THR199 4.8 9.2 1.0 CA A:THR214 4.8 11.9 1.0 CB A:SER96 4.9 11.1 1.0 NZ A:LYS213 5.0 4.6 1.0

N.Rhazi, P.Charlier, D.Dehareng, D.Engher, M.Vermeire, J.M.Frere, M.Nguyen-Disteche, E.Fonze. Catalytic Mechanism of the Streptomyces K15 Dd-Transpeptidase/Penicillin-Binding Protein Probed By Site-Directed Mutagenesis and Structural Analysis. Biochemistry V. 42 2895 2003.
ISSN: ISSN 0006-2960
PubMed: 12627955
DOI: 10.1021/BI027256X