Chlorine in PDB 4bl3: Crystal Structure of PBP2A Clinical Mutant N146K From Mrsa

All present enzymatic activity of Crystal Structure of PBP2A Clinical Mutant N146K From Mrsa:
3.4.16.4;

The structure of Crystal Structure of PBP2A Clinical Mutant N146K From Mrsa, PDB code: 4bl3 was solved by L.H.Otero, A.Rojas-Altuve, C.Carrasco-Lopez, J.A.Hermoso, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.74 / 3.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	81.790, 102.390, 187.130, 90.00, 90.00, 90.00
R / Rfree (%)	23.53 / 30.39

The structure of Crystal Structure of PBP2A Clinical Mutant N146K From Mrsa also contains other interesting chemical elements:

Cadmium

(Cd)

7 atoms

The binding sites of Chlorine atom in the Crystal Structure of PBP2A Clinical Mutant N146K From Mrsa (pdb code 4bl3). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Crystal Structure of PBP2A Clinical Mutant N146K From Mrsa, PDB code: 4bl3:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Crystal Structure of PBP2A Clinical Mutant N146K From Mrsa


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 PBP2A Clinical Mutant N146K From Mrsa within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1010 b:57.3 occ:1.00 CD A:CD1001 2.3 63.1 1.0 OE2 A:GLU145 3.1 64.8 1.0 OG1 A:THR300 3.2 53.2 1.0 OE1 B:GLU145 3.4 71.0 1.0 CG A:GLU145 3.4 64.7 1.0 ND1 A:HIS143 3.6 57.8 1.0 CD A:GLU145 3.7 64.7 1.0 CB A:HIS143 3.7 56.8 1.0 CG2 A:VAL302 4.0 60.3 1.0 CG A:HIS143 4.1 56.9 1.0 CD B:GLU145 4.4 71.1 1.0 CB A:THR300 4.4 53.3 1.0 CG1 A:ILE309 4.6 63.4 1.0 OE2 B:GLU145 4.6 71.2 1.0 CG2 A:THR300 4.7 53.4 1.0 CE1 A:HIS143 4.7 58.7 1.0 CB A:GLU145 4.8 64.4 1.0 OE1 A:GLU145 4.9 64.9 1.0

Chlorine binding site 2 out of 4 in the Crystal Structure of PBP2A Clinical Mutant N146K From Mrsa


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 PBP2A Clinical Mutant N146K From Mrsa within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1011 b:73.6 occ:1.00 CD A:CD1005 2.5 80.1 1.0 NE2 A:GLN137 3.5 64.4 1.0 OE1 A:GLN137 3.6 65.5 1.0 CD A:GLN137 3.6 67.7 1.0 CG B:GLN207 3.7 79.3 1.0 NE2 A:HIS311 3.7 64.2 1.0 NE2 A:GLN140 3.7 63.5 1.0 O A:GLY135 3.8 65.6 1.0 OD1 B:ASP209 3.8 75.2 1.0 CB B:GLN207 3.9 77.8 1.0 CB A:ALA310 4.2 66.0 1.0 CD2 A:HIS311 4.3 61.7 1.0 CG A:GLN137 4.4 70.4 1.0 OG1 B:THR210 4.4 73.4 1.0 CE1 A:HIS311 4.6 64.1 1.0 CD A:GLN140 4.6 60.0 1.0 OE1 A:GLN140 4.7 59.1 1.0 CD B:GLN207 4.7 78.4 1.0 CG B:ASP209 4.7 75.7 1.0 OD2 B:ASP209 4.8 76.6 1.0 CB A:GLN137 4.9 67.8 1.0 C A:GLY135 5.0 69.1 1.0

Chlorine binding site 3 out of 4 in the Crystal Structure of PBP2A Clinical Mutant N146K From Mrsa


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of PBP2A Clinical Mutant N146K From Mrsa within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1009 b:50.4 occ:1.00 CD B:CD1002 2.7 64.1 1.0 OG1 B:THR300 3.3 63.0 1.0 OE1 A:GLU145 3.6 64.9 1.0 CG1 B:ILE309 3.7 63.4 1.0 CG2 B:VAL302 3.7 67.0 1.0 CG B:GLU145 3.9 71.1 1.0 ND1 B:HIS143 3.9 69.6 1.0 OE2 B:GLU145 4.1 71.2 1.0 CD1 B:ILE309 4.1 64.0 1.0 CB B:THR300 4.2 64.3 1.0 CB B:HIS143 4.3 67.4 1.0 CD B:GLU145 4.3 71.1 1.0 CG2 B:THR300 4.4 64.2 1.0 CG B:HIS143 4.5 69.3 1.0 CD A:GLU145 4.6 64.7 1.0 OE2 A:GLU145 4.9 64.8 1.0 CE1 B:HIS143 5.0 71.0 1.0 NH1 B:ARG298 5.0 81.4 1.0

Chlorine binding site 4 out of 4 in the Crystal Structure of PBP2A Clinical Mutant N146K From Mrsa


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of PBP2A Clinical Mutant N146K From Mrsa within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1012 b:60.0 occ:1.00 CD A:CD1003 2.2 70.5 1.0 NE2 B:HIS311 3.0 64.5 1.0 O B:GLY135 3.4 57.0 1.0 CD2 B:HIS311 3.6 64.0 1.0 OD1 A:ASP209 3.7 67.2 1.0 NE2 B:GLN140 3.8 56.9 1.0 CB B:ALA310 3.9 64.6 1.0 CE1 B:HIS311 3.9 66.5 1.0 NE2 B:GLN137 4.0 66.3 1.0 CG A:GLN207 4.1 73.8 1.0 OG1 A:THR210 4.2 72.1 1.0 CD B:GLN137 4.2 67.8 1.0 OE1 B:GLN137 4.3 49.7 1.0 CB A:GLN207 4.4 72.1 1.0 OD2 A:ASP209 4.5 66.2 1.0 CG A:ASP209 4.5 66.9 1.0 C B:GLY135 4.6 57.1 1.0 CG B:HIS311 4.6 63.9 1.0 OE1 B:GLN140 4.6 59.6 1.0 O B:ALA310 4.6 64.6 1.0 CD B:GLN140 4.7 58.8 1.0 ND1 B:HIS311 4.8 65.9 1.0 CG B:GLN137 4.8 72.5 1.0 CA B:ALA310 4.9 64.1 1.0 C B:ALA310 4.9 64.2 1.0

J.Fishovitz, A.Rojas-Altuve, L.H.Otero, M.Dawley, C.Carrasco-Lopez, M.Chang, J.A.Hermoso, S.Mobashery. Disruption of Allosteric Response As An Unprecedented Mechanism of Resistance to Antibiotics. J.Am.Chem.Soc. V. 136 9814 2014.
ISSN: ISSN 0002-7863
PubMed: 24955778
DOI: 10.1021/JA5030657