Chlorine in PDB 5oe2: Crystal Structure of the Beta-Lactamase Oxa-245

All present enzymatic activity of Crystal Structure of the Beta-Lactamase Oxa-245:
3.5.2.6;

The structure of Crystal Structure of the Beta-Lactamase Oxa-245, PDB code: 5oe2 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)	45.26 / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	64.164, 108.720, 83.677, 90.00, 102.39, 90.00
R / Rfree (%)	19.1 / 22.6

The structure of Crystal Structure of the Beta-Lactamase Oxa-245 also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Chlorine atom in the Crystal Structure of the Beta-Lactamase Oxa-245 (pdb code 5oe2). 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 the Beta-Lactamase Oxa-245, PDB code: 5oe2:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of the Beta-Lactamase Oxa-245


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 the Beta-Lactamase Oxa-245 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:21.0 occ:1.00 HH12 A:ARG206 2.4 23.8 1.0 HH12 B:ARG206 2.4 22.8 1.0 HH22 B:ARG206 2.5 25.6 1.0 HH22 A:ARG206 2.6 22.9 1.0 NH1 B:ARG206 3.2 19.0 1.0 NH1 A:ARG206 3.2 19.8 1.0 O A:HOH517 3.2 49.7 1.0 NH2 B:ARG206 3.2 21.3 1.0 HD22 B:LEU196 3.3 31.6 1.0 NH2 A:ARG206 3.4 19.1 1.0 HA B:GLN193 3.4 28.4 1.0 HA A:GLN193 3.4 21.2 1.0 HD22 A:LEU196 3.5 29.1 1.0 CZ B:ARG206 3.6 25.4 1.0 HG3 B:GLN193 3.6 22.6 1.0 HG3 A:GLN193 3.7 21.3 1.0 CZ A:ARG206 3.7 25.9 1.0 HH11 A:ARG206 3.8 23.8 1.0 HH11 B:ARG206 3.9 22.8 1.0 HH21 B:ARG206 3.9 25.6 1.0 HH21 A:ARG206 4.1 22.9 1.0 HB2 B:LEU196 4.1 29.7 1.0 HB2 A:GLN193 4.2 23.7 1.0 CD2 B:LEU196 4.2 26.3 1.0 HB2 B:GLN193 4.2 26.0 1.0 HB2 A:LEU196 4.2 26.1 1.0 CA B:GLN193 4.3 23.7 1.0 CA A:GLN193 4.3 17.6 1.0 CD2 A:LEU196 4.5 24.2 1.0 CG B:GLN193 4.5 18.8 1.0 CG A:GLN193 4.5 17.8 1.0 HD13 B:LEU196 4.5 25.0 1.0 HD23 B:LEU196 4.5 31.6 1.0 CB A:GLN193 4.5 19.8 1.0 CB B:GLN193 4.5 21.6 1.0 HD13 A:LEU196 4.6 29.6 1.0 HD21 B:LEU196 4.7 31.6 1.0 HD23 A:LEU196 4.8 29.1 1.0 O B:GLN193 4.9 27.9 1.0 CB B:LEU196 4.9 24.8 1.0 HD21 A:LEU196 4.9 29.1 1.0 NE B:ARG206 4.9 26.4 1.0 O A:GLN193 5.0 22.2 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of the Beta-Lactamase Oxa-245


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 the Beta-Lactamase Oxa-245 within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl301 b:23.2 occ:1.00 HH22 C:ARG206 2.4 28.3 1.0 HH12 D:ARG206 2.4 18.2 1.0 HH22 D:ARG206 2.4 22.1 1.0 HH12 C:ARG206 2.5 25.3 1.0 NH1 D:ARG206 3.2 15.2 1.0 NH2 D:ARG206 3.2 18.4 1.0 NH2 C:ARG206 3.2 23.6 1.0 O C:HOH505 3.2 37.2 1.0 NH1 C:ARG206 3.2 21.1 1.0 HD21 D:LEU196 3.3 23.5 1.0 HA D:GLN193 3.3 26.2 1.0 O D:HOH416 3.4 39.3 1.0 HA C:GLN193 3.4 24.1 1.0 HD23 C:LEU196 3.4 26.5 1.0 CZ D:ARG206 3.6 22.7 1.0 HG3 C:GLN193 3.6 24.8 1.0 HG3 D:GLN193 3.6 27.5 1.0 CZ C:ARG206 3.6 26.5 1.0 HH11 D:ARG206 3.9 18.2 1.0 HH21 C:ARG206 3.9 28.3 1.0 HH21 D:ARG206 3.9 22.1 1.0 HH11 C:ARG206 3.9 25.3 1.0 HB2 D:LEU196 4.1 22.1 1.0 HB2 D:GLN193 4.1 28.5 1.0 HB2 C:GLN193 4.2 22.4 1.0 HB2 C:LEU196 4.2 23.0 1.0 CA D:GLN193 4.2 21.8 1.0 CD2 D:LEU196 4.3 19.6 1.0 CA C:GLN193 4.3 20.1 1.0 CD2 C:LEU196 4.3 22.1 1.0 CG C:GLN193 4.4 20.6 1.0 CG D:GLN193 4.5 22.9 1.0 CB D:GLN193 4.5 23.7 1.0 CB C:GLN193 4.5 18.6 1.0 HD22 D:LEU196 4.5 23.5 1.0 HD13 D:LEU196 4.5 24.4 1.0 HD21 C:LEU196 4.6 26.5 1.0 HD12 C:LEU196 4.6 27.2 1.0 HD23 D:LEU196 4.7 23.5 1.0 HD22 C:LEU196 4.8 26.5 1.0 NE D:ARG206 4.9 23.6 1.0 CB D:LEU196 4.9 18.4 1.0 NE C:ARG206 5.0 27.2 1.0 O D:GLN193 5.0 22.5 1.0 O C:GLN193 5.0 25.4 1.0

B.A.Lund, A.M.Thomassen, T.J.O.Carlsen, H.K.S.Leiros. Structure, Activity and Thermostability Investigations of Oxa-163, Oxa-181 and Oxa-245 Using Biochemical Analysis, Crystal Structures and Differential Scanning Calorimetry Analysis. Acta Crystallogr F Struct V. 73 579 2017BIOL Commun.
ISSN: ESSN 2053-230X
PubMed: 28994407
DOI: 10.1107/S2053230X17013838