Chlorine in PDB 1j9m: K38H Mutant of Streptomyces K15 Dd-Transpeptidase

All present enzymatic activity of K38H Mutant of Streptomyces K15 Dd-Transpeptidase:
3.4.16.4;

The structure of K38H Mutant of Streptomyces K15 Dd-Transpeptidase, PDB code: 1j9m was solved by E.Fonze, N.Rhazi, M.Nguyen-Disteche, P.Charlier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 1.65
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	45.596, 53.638, 104.690, 90.00, 90.00, 90.00
R / Rfree (%)	21.8 / 25.6

The structure of K38H Mutant of Streptomyces K15 Dd-Transpeptidase also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Chlorine atom in the K38H Mutant of Streptomyces K15 Dd-Transpeptidase (pdb code 1j9m). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the K38H Mutant of Streptomyces K15 Dd-Transpeptidase, PDB code: 1j9m:

Chlorine binding site 1 out of 1 in the K38H Mutant of Streptomyces K15 Dd-Transpeptidase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of K38H Mutant of Streptomyces K15 Dd-Transpeptidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl601 b:33.2 occ:1.00 NA A:NA600 2.8 24.5 1.0 OG A:SER216 3.0 18.7 1.0 NH1 A:ARG248 3.2 14.4 1.0 CB A:SER216 3.3 16.3 1.0 NH2 A:ARG248 3.4 16.3 1.0 C A:GLY215 3.7 10.4 1.0 CZ A:ARG248 3.8 15.0 1.0 N A:SER216 3.8 13.3 1.0 O A:GLY215 3.8 11.4 1.0 N A:GLY215 4.0 10.5 1.0 CA A:GLY215 4.1 10.9 1.0 OG1 A:THR214 4.2 10.3 1.0 CA A:SER216 4.2 13.9 1.0 CB A:THR214 4.3 11.4 1.0 O A:HOH332 4.3 21.9 1.0 OG A:SER35 4.6 20.2 1.0 C A:THR214 4.7 11.4 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