Chlorine in PDB 5qaz: Oxa-48 in Complex with Compound 34

All present enzymatic activity of Oxa-48 in Complex with Compound 34:
3.5.2.6;

The structure of Oxa-48 in Complex with Compound 34, PDB code: 5qaz was solved by B.A.Lund, H.K.S.Leiros, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.17 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	88.997, 108.495, 125.123, 90.00, 90.00, 90.00
R / Rfree (%)	20.8 / 26.7

The binding sites of Chlorine atom in the Oxa-48 in Complex with Compound 34 (pdb code 5qaz). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Oxa-48 in Complex with Compound 34, PDB code: 5qaz:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Oxa-48 in Complex with Compound 34


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Oxa-48 in Complex with Compound 34 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl302 b:21.9 occ:1.00 HH22 B:ARG206 2.1 14.7 1.0 HH12 B:ARG206 2.3 15.9 1.0 O B:HOH546 2.5 27.1 1.0 NH2 B:ARG206 2.9 12.2 1.0 NH1 B:ARG206 3.1 13.2 1.0 HA B:GLN193 3.3 13.5 1.0 HG3 B:GLN193 3.3 20.1 1.0 HD21 B:LEU196 3.3 25.1 1.0 CZ B:ARG206 3.4 8.2 1.0 HH21 B:ARG206 3.6 14.7 1.0 HH11 B:ARG206 3.8 15.9 1.0 HB2 B:GLN193 4.1 15.8 1.0 HB2 B:LEU196 4.1 19.8 1.0 CA B:GLN193 4.2 11.2 1.0 CG B:GLN193 4.2 16.7 1.0 CD2 B:LEU196 4.3 20.9 1.0 CB B:GLN193 4.4 13.1 1.0 HD12 B:LEU196 4.6 19.3 1.0 HD22 B:LEU196 4.6 25.1 1.0 O B:HOH433 4.7 31.6 1.0 HG2 B:GLN193 4.7 20.1 1.0 NE B:ARG206 4.8 11.8 1.0 HD23 B:LEU196 4.8 25.1 1.0 O B:HOH581 4.9 33.4 1.0 O B:GLN193 4.9 18.0 1.0 CB B:LEU196 5.0 16.5 1.0

Chlorine binding site 2 out of 2 in the Oxa-48 in Complex with Compound 34


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Oxa-48 in Complex with Compound 34 within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl302 b:23.8 occ:1.00 HH12 C:ARG206 2.3 19.3 1.0 HH22 C:ARG206 2.5 17.9 1.0 NH1 C:ARG206 3.0 16.0 1.0 NH2 C:ARG206 3.2 14.9 1.0 HA C:GLN193 3.2 15.7 1.0 HG3 C:GLN193 3.3 21.8 1.0 HD22 C:LEU196 3.4 25.7 1.0 CZ C:ARG206 3.5 12.4 1.0 HH11 C:ARG206 3.7 19.3 1.0 HH21 C:ARG206 3.9 17.9 1.0 HB2 C:GLN193 4.0 19.3 1.0 CA C:GLN193 4.1 13.1 1.0 CG C:GLN193 4.1 18.1 1.0 HB2 C:LEU196 4.2 25.4 1.0 CB C:GLN193 4.3 16.0 1.0 CD2 C:LEU196 4.4 21.4 1.0 O C:HOH526 4.5 40.9 1.0 HD12 C:LEU196 4.6 8.9 1.0 HG2 C:GLN193 4.7 21.8 1.0 HD23 C:LEU196 4.7 25.7 1.0 O C:GLN193 4.8 11.0 1.0 NE C:ARG206 4.9 14.5 1.0 HD21 C:LEU196 4.9 25.7 1.0 N C:GLN193 4.9 19.3 1.0 CB C:LEU196 5.0 21.1 1.0

S.Akhter, B.A.Lund, A.Ismael, M.Langer, J.Isaksson, T.Christopeit, H.S.Leiros, A.Bayer. A Focused Fragment Library Targeting the Antibiotic Resistance Enzyme - Oxacillinase-48: Synthesis, Structural Evaluation and Inhibitor Design. Eur J Med Chem V. 145 634 2018.
ISSN: ISSN 1768-3254
PubMed: 29348071
DOI: 10.1016/J.EJMECH.2017.12.085