Chlorine in PDB 5qay: Oxa-48 in Complex with Compound 32

All present enzymatic activity of Oxa-48 in Complex with Compound 32:
3.5.2.6;

The structure of Oxa-48 in Complex with Compound 32, PDB code: 5qay 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)	43.49 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	89.722, 108.403, 124.870, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 23.9

The binding sites of Chlorine atom in the Oxa-48 in Complex with Compound 32 (pdb code 5qay). 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 32, PDB code: 5qay:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Oxa-48 in Complex with Compound 32


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 32 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl302 b:20.5 occ:0.96 HH12 C:ARG206 2.4 33.5 1.0 HH22 C:ARG206 2.5 27.7 1.0 HH12 A:ARG206 2.5 29.9 1.0 HH22 A:ARG206 2.6 20.9 1.0 O A:HOH591 3.1 62.4 1.0 NH1 C:ARG206 3.2 27.9 1.0 NH2 C:ARG206 3.2 23.1 1.0 NH1 A:ARG206 3.3 24.9 1.0 NH2 A:ARG206 3.3 17.4 1.0 HD21 A:LEU196 3.3 27.8 1.0 HD22 C:LEU196 3.3 24.2 1.0 HA A:GLN193 3.3 22.8 1.0 HA C:GLN193 3.3 24.0 1.0 HG3 A:GLN193 3.4 26.3 1.0 HG3 C:GLN193 3.5 24.6 1.0 CZ C:ARG206 3.6 23.0 1.0 CZ A:ARG206 3.7 21.1 1.0 HH11 C:ARG206 3.9 33.5 1.0 HH11 A:ARG206 3.9 29.9 1.0 HH21 C:ARG206 3.9 27.7 1.0 HH21 A:ARG206 4.0 20.9 1.0 HB2 A:LEU196 4.0 25.8 1.0 HB2 C:LEU196 4.0 19.2 1.0 HB2 C:GLN193 4.2 22.7 1.0 HB2 A:GLN193 4.2 20.4 1.0 CA A:GLN193 4.2 18.9 1.0 CA C:GLN193 4.2 20.0 1.0 CD2 A:LEU196 4.3 23.1 1.0 CG A:GLN193 4.3 21.9 1.0 CD2 C:LEU196 4.3 20.2 1.0 HD11 C:LEU196 4.4 27.6 1.0 CG C:GLN193 4.4 20.4 1.0 CB A:GLN193 4.5 16.9 1.0 CB C:GLN193 4.5 18.9 1.0 HD12 A:LEU196 4.5 26.6 1.0 HD22 A:LEU196 4.5 27.8 1.0 HD23 C:LEU196 4.7 24.2 1.0 HD23 A:LEU196 4.7 27.8 1.0 HD21 C:LEU196 4.8 24.2 1.0 HG2 A:GLN193 4.8 26.3 1.0 CB A:LEU196 4.8 21.5 1.0 CB C:LEU196 4.9 16.0 1.0 O A:GLN193 4.9 20.5 1.0 O A:HOH497 4.9 39.0 1.0 HG2 C:GLN193 4.9 24.6 1.0 NE C:ARG206 5.0 17.6 1.0 NE A:ARG206 5.0 20.3 1.0 O C:HOH486 5.0 47.9 1.0 O C:GLN193 5.0 19.3 1.0

Chlorine binding site 2 out of 2 in the Oxa-48 in Complex with Compound 32


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 32 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl302 b:19.6 occ:1.00 HH22 D:ARG206 2.4 22.2 1.0 HH12 D:ARG206 2.5 26.6 1.0 HH12 B:ARG206 2.5 27.6 1.0 HH22 B:ARG206 2.5 23.3 1.0 NH2 D:ARG206 3.2 18.6 1.0 NH1 D:ARG206 3.2 22.1 1.0 NH1 B:ARG206 3.2 23.0 1.0 O B:HOH591 3.2 38.7 1.0 NH2 B:ARG206 3.2 19.4 1.0 HA D:GLN193 3.3 24.6 1.0 HD22 B:LEU196 3.3 27.3 1.0 HA B:GLN193 3.4 23.8 1.0 HD22 D:LEU196 3.4 26.7 1.0 HG3 B:GLN193 3.5 27.8 1.0 HG3 D:GLN193 3.5 22.8 1.0 CZ D:ARG206 3.6 21.5 1.0 CZ B:ARG206 3.7 23.2 1.0 HH21 D:ARG206 3.8 22.2 1.0 HH11 B:ARG206 3.9 27.6 1.0 HH11 D:ARG206 3.9 26.6 1.0 HH21 B:ARG206 3.9 23.3 1.0 HB2 D:LEU196 4.1 25.3 1.0 HB2 B:LEU196 4.1 23.7 1.0 HB2 D:GLN193 4.2 28.8 1.0 HB2 B:GLN193 4.2 25.1 1.0 CA D:GLN193 4.2 20.4 1.0 CA B:GLN193 4.3 19.8 1.0 CD2 B:LEU196 4.3 22.8 1.0 CG B:GLN193 4.4 23.1 1.0 CG D:GLN193 4.4 19.0 1.0 CD2 D:LEU196 4.4 22.2 1.0 HD12 D:LEU196 4.4 27.5 1.0 CB D:GLN193 4.5 24.0 1.0 CB B:GLN193 4.5 20.9 1.0 HD12 B:LEU196 4.5 29.6 1.0 HD23 B:LEU196 4.5 27.3 1.0 HD23 D:LEU196 4.8 26.7 1.0 HD21 B:LEU196 4.8 27.3 1.0 HD21 D:LEU196 4.9 26.7 1.0 CB D:LEU196 4.9 21.1 1.0 CB B:LEU196 4.9 19.7 1.0 HG2 B:GLN193 4.9 27.8 1.0 NE D:ARG206 4.9 21.3 1.0 O B:HOH466 4.9 37.9 1.0 O D:GLN193 4.9 21.0 1.0 NE B:ARG206 5.0 19.2 1.0 HG2 D:GLN193 5.0 22.8 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