Chlorine in PDB 7lxg: Homocitrullinated Beta-Lactamase Oxa-48

All present enzymatic activity of Homocitrullinated Beta-Lactamase Oxa-48:
3.5.2.6;

The structure of Homocitrullinated Beta-Lactamase Oxa-48, PDB code: 7lxg was solved by J.E.Serrano-Negron, D.T.King, D.J.Vocadlo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.12 / 2.20
Space group	P 62
Cell size a, b, c (Å), α, β, γ (°)	143.96, 143.96, 56.03, 90, 90, 120
R / Rfree (%)	16.8 / 21.7

The binding sites of Chlorine atom in the Homocitrullinated Beta-Lactamase Oxa-48 (pdb code 7lxg). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Homocitrullinated Beta-Lactamase Oxa-48, PDB code: 7lxg:

Chlorine binding site 1 out of 1 in the Homocitrullinated Beta-Lactamase Oxa-48


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Homocitrullinated Beta-Lactamase Oxa-48 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl302 b:42.0 occ:1.00 HH12 A:ARG206 2.3 47.2 1.0 HH12 B:ARG206 2.4 42.7 1.0 HH22 A:ARG206 2.6 42.1 1.0 HH22 B:ARG206 2.7 43.3 1.0 NH1 A:ARG206 3.1 39.3 1.0 NH1 B:ARG206 3.2 35.6 1.0 NH2 A:ARG206 3.3 35.1 1.0 HD22 B:LEU196 3.3 44.2 1.0 HD22 A:LEU196 3.3 45.9 1.0 NH2 B:ARG206 3.4 36.1 1.0 HA A:GLN193 3.4 50.9 1.0 HA B:GLN193 3.4 53.7 1.0 HG3 B:GLN193 3.6 51.9 1.0 CZ A:ARG206 3.6 38.1 1.0 HG3 A:GLN193 3.7 54.9 1.0 CZ B:ARG206 3.8 39.5 1.0 HH11 A:ARG206 3.8 47.2 1.0 HH11 B:ARG206 3.8 42.7 1.0 HB2 B:LEU196 4.0 42.6 1.0 HH21 A:ARG206 4.0 42.1 1.0 HB2 A:LEU196 4.0 48.2 1.0 HB2 B:GLN193 4.1 46.4 1.0 HD13 B:LEU196 4.1 39.9 1.0 HH21 B:ARG206 4.2 43.3 1.0 CD2 B:LEU196 4.2 36.8 1.0 HD13 A:LEU196 4.3 47.7 1.0 HD23 B:LEU196 4.3 44.2 1.0 CD2 A:LEU196 4.3 38.3 1.0 CA B:GLN193 4.3 44.8 1.0 CA A:GLN193 4.3 42.4 1.0 HB2 A:GLN193 4.3 47.5 1.0 CG B:GLN193 4.4 43.3 1.0 CB B:GLN193 4.5 38.7 1.0 CG A:GLN193 4.6 45.7 1.0 CB A:GLN193 4.6 39.6 1.0 HD21 A:LEU196 4.7 45.9 1.0 HD23 A:LEU196 4.8 45.9 1.0 CB B:LEU196 4.8 35.5 1.0 HD21 B:LEU196 4.8 44.2 1.0 CB A:LEU196 4.9 40.1 1.0 CG B:LEU196 4.9 34.1 1.0 HG2 B:GLN193 4.9 51.9 1.0 CD1 B:LEU196 4.9 33.3 1.0 NE A:ARG206 4.9 38.0 1.0 O A:GLN193 4.9 39.6 1.0 CG A:LEU196 5.0 39.5 1.0 CD1 A:LEU196 5.0 39.8 1.0

D.T.King, S.Zhu, D.B.Hardie, J.E.Serrano-Negron, Z.Madden, S.Kolappan, D.J.Vocadlo. Chemoproteomic Identification of Co 2 -Dependent Lysine Carboxylation in Proteins. Nat.Chem.Biol. V. 18 782 2022.
ISSN: ESSN 1552-4469
PubMed: 35710617
DOI: 10.1038/S41589-022-01043-1