Chlorine in PDB 5qa5: Oxa-48 in Complex with Compound 3B

All present enzymatic activity of Oxa-48 in Complex with Compound 3B:
3.5.2.6;

The structure of Oxa-48 in Complex with Compound 3B, PDB code: 5qa5 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)	43.62 / 1.95
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	89.341, 109.061, 124.906, 90.00, 90.00, 90.00
R / Rfree (%)	15.5 / 19.3

The binding sites of Chlorine atom in the Oxa-48 in Complex with Compound 3B (pdb code 5qa5). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Oxa-48 in Complex with Compound 3B, PDB code: 5qa5:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Oxa-48 in Complex with Compound 3B


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 3B within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl302 b:26.4 occ:1.00 HH22 C:ARG206 2.2 23.8 1.0 O C:HOH594 2.4 30.1 1.0 HH12 C:ARG206 2.4 22.0 1.0 NH2 C:ARG206 3.0 19.8 1.0 NH1 C:ARG206 3.1 18.3 1.0 HA C:GLN193 3.4 17.9 1.0 HD22 C:LEU196 3.4 30.8 1.0 CZ C:ARG206 3.5 16.6 1.0 HG3 C:GLN193 3.6 19.1 1.0 HH21 C:ARG206 3.6 23.8 1.0 HH11 C:ARG206 3.8 22.0 1.0 HB2 C:LEU196 4.1 18.2 1.0 HB2 C:GLN193 4.2 19.5 1.0 CA C:GLN193 4.3 15.1 1.0 CD2 C:LEU196 4.4 25.6 1.0 CG C:GLN193 4.5 16.2 1.0 CB C:GLN193 4.5 16.2 1.0 HD13 C:LEU196 4.5 18.6 1.0 O C:HOH538 4.6 41.6 1.0 HD23 C:LEU196 4.7 30.8 1.0 NE C:ARG206 4.8 15.7 1.0 HD21 C:LEU196 4.8 30.8 1.0 CB C:LEU196 5.0 15.4 1.0 O C:GLN193 5.0 20.1 1.0

Chlorine binding site 2 out of 3 in the Oxa-48 in Complex with Compound 3B


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 3B within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl302 b:56.0 occ:1.00 O D:HOH418 2.8 25.4 1.0 O D:LEU228 2.9 19.0 1.0 O D:HOH629 3.0 37.0 1.0 HG23 D:VAL232 3.2 22.5 0.8 HG22 D:VAL232 3.3 22.5 0.8 O D:ASN231 3.3 17.4 1.0 O D:HOH514 3.5 26.8 1.0 HH D:TYR177 3.6 28.6 1.0 H D:ASN231 3.6 23.4 1.0 CG2 D:VAL232 3.7 18.7 0.8 O D:HOH482 3.8 39.2 1.0 HB3 D:GLU227 3.9 23.4 1.0 HB D:VAL232 3.9 25.5 0.2 C D:ASN231 3.9 25.9 1.0 H D:LEU228 3.9 21.2 1.0 N D:ASN231 4.0 19.4 1.0 OH D:TYR177 4.0 23.8 1.0 HG21 D:VAL232 4.1 22.5 0.8 C D:LEU228 4.1 19.4 1.0 O D:HOH457 4.1 46.9 1.0 O D:ASP229 4.2 24.1 1.0 HA D:GLU227 4.3 17.9 1.0 N D:LEU228 4.4 17.6 1.0 C D:ASP229 4.4 22.3 1.0 CA D:ASN231 4.5 22.3 1.0 HA D:ASN231 4.6 26.8 1.0 N D:VAL232 4.7 16.5 0.8 N D:VAL232 4.7 23.8 0.2 N D:ASP230 4.7 22.4 1.0 CB D:GLU227 4.7 19.4 1.0 C D:ASP230 4.8 28.4 1.0 CB D:VAL232 4.8 21.2 0.2 HG2 D:GLU227 4.8 25.6 1.0 HA D:ASP230 4.9 33.5 1.0 CA D:GLU227 4.9 15.2 1.0 HA D:VAL232 4.9 18.9 0.8 CA D:LEU228 4.9 23.6 1.0 HA D:ASP229 4.9 24.5 1.0 HA D:VAL232 4.9 22.8 0.2

Chlorine binding site 3 out of 3 in the Oxa-48 in Complex with Compound 3B


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Oxa-48 in Complex with Compound 3B within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl303 b:26.3 occ:1.00 HH12 D:ARG206 2.3 16.5 1.0 HH22 D:ARG206 2.4 17.8 1.0 NH1 D:ARG206 3.1 14.0 1.0 NH2 D:ARG206 3.2 14.8 1.0 HA D:GLN193 3.3 28.8 1.0 HD22 D:LEU196 3.5 22.5 1.0 HG3 D:GLN193 3.5 21.6 1.0 CZ D:ARG206 3.6 18.0 1.0 HH11 D:ARG206 3.8 16.5 1.0 HH21 D:ARG206 3.9 17.8 1.0 HB2 D:GLN193 4.1 19.1 1.0 HB2 D:LEU196 4.2 19.2 1.0 CA D:GLN193 4.2 23.9 1.0 CG D:GLN193 4.4 17.9 1.0 CD2 D:LEU196 4.5 18.7 1.0 CB D:GLN193 4.5 15.8 1.0 HD13 D:LEU196 4.6 23.9 1.0 O D:HOH479 4.8 36.0 1.0 HD23 D:LEU196 4.8 22.5 1.0 NE D:ARG206 4.9 17.2 1.0 HD21 D:LEU196 4.9 22.5 1.0 O D:GLN193 5.0 17.5 1.0 HG2 D:GLN193 5.0 21.6 1.0 O D:HOH602 5.0 32.8 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