Chlorine in PDB 6hb8: Crystal Structure of Oxa-517 Beta-Lactamase

All present enzymatic activity of Crystal Structure of Oxa-517 Beta-Lactamase:
3.5.2.6;

The structure of Crystal Structure of Oxa-517 Beta-Lactamase, PDB code: 6hb8 was solved by J.E.Raczynska, L.Dabos, A.Zavala, P.Retailleau, B.Iorga, M.Jaskolski, T.Naas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.18 / 1.86
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.800, 125.046, 82.656, 90.00, 94.65, 90.00
R / Rfree (%)	17 / 21.9

The binding sites of Chlorine atom in the Crystal Structure of Oxa-517 Beta-Lactamase (pdb code 6hb8). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Oxa-517 Beta-Lactamase, PDB code: 6hb8:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Oxa-517 Beta-Lactamase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Oxa-517 Beta-Lactamase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl305 b:37.0 occ:0.50 O1 D:SO4303 1.0 34.6 0.5 O2 D:SO4303 1.4 35.9 0.5 S D:SO4303 1.4 34.9 0.5 O4 D:SO4303 2.5 33.5 0.5 O3 D:SO4303 2.6 30.5 0.5 NH2 A:ARG206 2.9 27.7 1.0 NH2 D:ARG206 3.0 31.8 1.0 NH1 D:ARG206 3.0 29.1 1.0 NH1 A:ARG206 3.1 26.7 1.0 CZ A:ARG206 3.4 27.8 1.0 CZ D:ARG206 3.4 28.5 1.0 CD2 D:LEU196 4.1 33.7 1.0 CD2 A:LEU196 4.1 30.7 1.0 CG D:GLN193 4.2 36.7 1.0 CA D:GLN193 4.3 32.6 1.0 CA A:GLN193 4.4 30.6 1.0 CG A:GLN193 4.4 35.7 1.0 CB D:GLN193 4.5 29.4 1.0 CB A:GLN193 4.6 34.8 1.0 NE A:ARG206 4.7 32.1 1.0 NE D:ARG206 4.8 33.3 1.0 CB D:LEU196 4.8 33.5 1.0 CG D:LEU196 4.9 32.2 1.0 CB A:LEU196 4.9 32.0 1.0 CG A:LEU196 4.9 29.9 1.0 O D:HOH402 5.0 48.4 1.0 O D:HOH410 5.0 38.9 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Oxa-517 Beta-Lactamase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Oxa-517 Beta-Lactamase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl306 b:33.9 occ:0.50 O1 B:SO4303 1.2 39.4 0.5 O2 B:SO4303 1.3 40.6 0.5 S B:SO4303 1.4 36.5 0.5 O4 B:SO4303 2.5 34.6 0.5 O3 B:SO4303 2.5 34.2 0.5 NH2 B:ARG206 2.9 27.8 1.0 NH1 B:ARG206 3.0 28.1 1.0 NH1 C:ARG206 3.0 28.7 1.0 NH2 C:ARG206 3.1 27.6 1.0 CZ B:ARG206 3.4 31.6 1.0 CZ C:ARG206 3.5 29.6 1.0 CD2 C:LEU196 4.1 34.4 1.0 CD2 B:LEU196 4.2 32.8 1.0 CG C:GLN193 4.3 32.4 1.0 CA C:GLN193 4.3 29.4 1.0 CG B:GLN193 4.3 39.2 1.0 CA B:GLN193 4.4 32.9 1.0 CB C:GLN193 4.5 31.8 1.0 CB B:GLN193 4.6 34.0 1.0 O B:HOH475 4.7 63.3 1.0 NE B:ARG206 4.7 31.1 1.0 NE C:ARG206 4.8 30.6 1.0 CB C:LEU196 4.8 35.1 1.0 CG C:LEU196 4.9 31.9 1.0 CB B:LEU196 4.9 29.0 1.0 CG B:LEU196 4.9 33.8 1.0 O B:HOH408 4.9 46.6 1.0 O B:HOH406 4.9 49.4 1.0 O C:GLN193 5.0 32.0 1.0

L.Dabos, J.E.Raczynska, P.Bogaerts, A.Zavala, R.A.Bonnin, A.Peyrat, P.Retailleau, B.Iorga, M.Jaskolski, Y.Glupczynski, T.Naas. Genetic, Biochemical and Structural Characterization of Oxa-517, An Oxa-48-Like Extended-Spectrum Cephalosporins and Carbapenems-Hydrolyzing Beta-Lactamase To Be Published.