Chlorine in PDB 5qa9: Oxa-48 in Complex with Compound 5

All present enzymatic activity of Oxa-48 in Complex with Compound 5:
3.5.2.6;

The structure of Oxa-48 in Complex with Compound 5, PDB code: 5qa9 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)	43.38 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	88.981, 108.447, 124.139, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 23

The binding sites of Chlorine atom in the Oxa-48 in Complex with Compound 5 (pdb code 5qa9). 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 5, PDB code: 5qa9:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Oxa-48 in Complex with Compound 5


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 5 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl302 b:18.0 occ:1.00 HH22 A:ARG206 2.3 22.6 1.0 HH12 A:ARG206 2.4 21.8 1.0 O A:HOH657 3.0 44.9 1.0 NH2 A:ARG206 3.1 18.8 1.0 NH1 A:ARG206 3.1 18.1 1.0 HA A:GLN193 3.3 19.2 1.0 CZ A:ARG206 3.5 21.5 1.0 HD22 A:LEU196 3.5 21.2 1.0 HG3 A:GLN193 3.6 23.1 1.0 HH21 A:ARG206 3.8 22.6 1.0 HH11 A:ARG206 3.8 21.8 1.0 HB2 A:GLN193 4.0 19.9 1.0 CA A:GLN193 4.2 16.3 1.0 HB2 A:LEU196 4.2 19.5 1.0 CB A:GLN193 4.4 16.5 1.0 CG A:GLN193 4.4 19.2 1.0 HD13 A:LEU196 4.5 20.2 1.0 CD2 A:LEU196 4.5 17.6 1.0 O A:HOH429 4.8 47.3 1.0 NE A:ARG206 4.8 19.3 1.0 HD23 A:LEU196 4.9 21.2 1.0 HD21 A:LEU196 5.0 21.2 1.0 O A:GLN193 5.0 17.6 1.0 N A:GLN193 5.0 18.9 1.0

Chlorine binding site 2 out of 2 in the Oxa-48 in Complex with Compound 5


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 5 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl302 b:16.6 occ:1.00 HH22 B:ARG206 2.3 18.9 1.0 HH12 B:ARG206 2.4 18.7 1.0 O B:HOH627 2.9 38.3 1.0 NH2 B:ARG206 3.1 15.7 1.0 NH1 B:ARG206 3.2 15.5 1.0 HA B:GLN193 3.2 20.6 1.0 HD22 B:LEU196 3.5 15.9 1.0 HG3 B:GLN193 3.6 15.3 1.0 CZ B:ARG206 3.6 18.2 1.0 HH21 B:ARG206 3.8 18.9 1.0 HH11 B:ARG206 3.9 18.7 1.0 HB2 B:GLN193 3.9 17.4 1.0 CA B:GLN193 4.1 17.1 1.0 HB2 B:LEU196 4.2 19.7 1.0 CB B:GLN193 4.3 14.4 1.0 CG B:GLN193 4.4 12.7 1.0 HD13 B:LEU196 4.4 20.3 1.0 CD2 B:LEU196 4.5 13.2 1.0 O B:HOH456 4.7 32.2 1.0 HD23 B:LEU196 4.8 15.9 1.0 NE B:ARG206 4.9 18.0 1.0 O B:GLN193 4.9 13.4 1.0 HD21 B:LEU196 4.9 15.9 1.0 N B:GLN193 4.9 17.0 1.0 HG2 B:GLN193 5.0 15.3 1.0 CB B:LEU196 5.0 16.4 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