Chlorine in PDB 1fsy: Ampc Beta-Lactamase From E. Coli Complexed with Inhibitor Cloxacillinboronic Acid

All present enzymatic activity of Ampc Beta-Lactamase From E. Coli Complexed with Inhibitor Cloxacillinboronic Acid:
3.5.2.6;

The structure of Ampc Beta-Lactamase From E. Coli Complexed with Inhibitor Cloxacillinboronic Acid, PDB code: 1fsy was solved by E.Caselli, R.A.Powers, L.C.Blasczcak, C.Y.Wu, F.Prati, B.K.Shoichet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.75
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	118.360, 77.570, 97.460, 90.00, 116.18, 90.00
R / Rfree (%)	19.6 / 21.8

The binding sites of Chlorine atom in the Ampc Beta-Lactamase From E. Coli Complexed with Inhibitor Cloxacillinboronic Acid (pdb code 1fsy). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Ampc Beta-Lactamase From E. Coli Complexed with Inhibitor Cloxacillinboronic Acid, PDB code: 1fsy:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Ampc Beta-Lactamase From E. Coli Complexed with Inhibitor Cloxacillinboronic Acid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Ampc Beta-Lactamase From E. Coli Complexed with Inhibitor Cloxacillinboronic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl964 b:44.5 occ:1.00 CL1 A:105964 0.0 44.5 1.0 C14 A:105964 1.8 44.1 1.0 C15 A:105964 2.8 44.8 1.0 C13 A:105964 2.8 43.4 1.0 C12 A:105964 3.2 41.4 1.0 C5 A:105964 3.4 37.8 1.0 C7 A:105964 3.5 39.8 1.0 O6 A:105964 3.6 39.3 1.0 CD A:GLN120 3.7 37.1 1.0 CG A:GLN120 3.8 33.5 1.0 N4 A:105964 3.8 35.0 1.0 NE2 A:GLN120 3.9 39.1 1.0 CD2 A:LEU119 3.9 27.0 1.0 OE1 A:GLN120 4.0 37.8 1.0 N11 A:105964 4.1 42.0 1.0 C16 A:105964 4.1 45.7 1.0 CG A:LEU119 4.1 25.2 1.0 C18 A:105964 4.1 44.1 1.0 O A:HOH867 4.1 44.5 1.0 C8 A:105964 4.4 40.2 1.0 CD1 A:LEU119 4.4 26.0 1.0 C3 A:105964 4.5 28.0 1.0 ND2 A:ASN152 4.6 21.2 1.0 C17 A:105964 4.6 44.8 1.0 O10 A:105964 4.8 41.5 1.0

Chlorine binding site 2 out of 2 in the Ampc Beta-Lactamase From E. Coli Complexed with Inhibitor Cloxacillinboronic Acid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Ampc Beta-Lactamase From E. Coli Complexed with Inhibitor Cloxacillinboronic Acid within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl964 b:56.8 occ:1.00 CL1 B:105964 0.0 56.8 1.0 C14 B:105964 1.8 54.2 1.0 C15 B:105964 2.8 55.2 1.0 C13 B:105964 2.9 52.9 1.0 C12 B:105964 3.2 50.1 1.0 C5 B:105964 3.4 44.2 1.0 C7 B:105964 3.5 47.6 1.0 O6 B:105964 3.6 45.1 1.0 CD B:GLN120 3.6 40.6 1.0 NE2 B:GLN120 3.7 42.1 1.0 CG B:GLN120 3.8 38.1 1.0 N4 B:105964 3.9 39.3 1.0 OE1 B:GLN120 3.9 43.5 1.0 CD2 B:LEU119 4.0 27.7 1.0 C16 B:105964 4.1 55.3 1.0 N11 B:105964 4.2 50.4 1.0 C18 B:105964 4.2 53.7 1.0 CG B:LEU119 4.2 25.9 1.0 C8 B:105964 4.5 49.0 1.0 C3 B:105964 4.6 31.7 1.0 CD1 B:LEU119 4.6 27.8 1.0 ND2 B:ASN152 4.6 28.2 1.0 C17 B:105964 4.7 55.0 1.0 O10 B:105964 4.9 49.9 1.0

E.Caselli, R.A.Powers, L.C.Blasczcak, C.Y.Wu, F.Prati, B.K.Shoichet. Energetic, Structural, and Antimicrobial Analyses of Beta-Lactam Side Chain Recognition By Beta-Lactamases. Chem.Biol. V. 8 17 2001.
ISSN: ISSN 1074-5521
PubMed: 11182316
DOI: 10.1016/S1074-5521(00)00052-1