Chlorine in PDB 4kqr: Crystal Structure of Penicillin-Binding Protein 3 From Pseudomonas Aeruginosa in Complex with (5S)-Penicilloic Acid

The structure of Crystal Structure of Penicillin-Binding Protein 3 From Pseudomonas Aeruginosa in Complex with (5S)-Penicilloic Acid, PDB code: 4kqr was solved by J.E.Nettleship, D.I.Stuart, R.J.Owens, J.Ren, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.36 / 2.01
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	57.199, 75.453, 83.218, 70.77, 85.40, 85.06
R / Rfree (%)	18.5 / 20.7

The binding sites of Chlorine atom in the Crystal Structure of Penicillin-Binding Protein 3 From Pseudomonas Aeruginosa in Complex with (5S)-Penicilloic Acid (pdb code 4kqr). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 5 binding sites of Chlorine where determined in the Crystal Structure of Penicillin-Binding Protein 3 From Pseudomonas Aeruginosa in Complex with (5S)-Penicilloic Acid, PDB code: 4kqr:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5;

Chlorine binding site 1 out of 5 in the Crystal Structure of Penicillin-Binding Protein 3 From Pseudomonas Aeruginosa in Complex with (5S)-Penicilloic Acid


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 Penicillin-Binding Protein 3 From Pseudomonas Aeruginosa in Complex with (5S)-Penicilloic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl602 b:38.7 occ:1.00 N A:ASN501 3.2 29.3 1.0 O A:HOH892 3.4 42.0 1.0 NE A:ARG499 3.5 29.3 1.0 CA A:ASN501 3.7 28.8 1.0 NH1 A:ARG499 3.7 29.2 1.0 C A:ASN501 3.7 24.9 1.0 CB A:ARG499 3.8 27.3 1.0 CB A:ASN501 3.9 31.8 1.0 N A:ALA502 3.9 21.9 1.0 N A:GLU500 3.9 30.4 1.0 CZ A:ARG499 4.1 29.5 1.0 CB A:ALA502 4.2 19.1 1.0 O A:ASN501 4.2 25.6 1.0 C A:GLU500 4.3 30.9 1.0 C A:ARG499 4.4 27.7 1.0 CG A:ARG499 4.5 28.0 1.0 CA A:ARG499 4.5 26.7 1.0 CA A:GLU500 4.5 33.1 1.0 CD A:ARG499 4.6 28.5 1.0 OD1 A:ASN501 4.6 38.8 1.0 CA A:ALA502 4.7 19.1 1.0 CG A:ASN501 4.7 35.2 1.0 CB A:GLU500 4.8 37.2 1.0

Chlorine binding site 2 out of 5 in the Crystal Structure of Penicillin-Binding Protein 3 From Pseudomonas Aeruginosa in Complex with (5S)-Penicilloic Acid


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 Penicillin-Binding Protein 3 From Pseudomonas Aeruginosa in Complex with (5S)-Penicilloic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl603 b:38.3 occ:1.00 N A:GLY494 3.1 24.7 1.0 NH1 B:ARG233 3.2 21.5 1.0 CA A:VAL493 3.5 27.1 1.0 CG1 A:VAL493 3.7 29.2 1.0 CA B:LEU230 3.7 16.6 1.0 CD B:ARG233 3.8 19.4 1.0 C A:VAL493 3.8 26.8 1.0 CD1 B:LEU230 4.0 19.5 1.0 N B:LEU230 4.0 15.9 1.0 O B:HOH809 4.1 42.6 1.0 CB B:LEU230 4.1 17.8 1.0 O A:SER492 4.1 23.6 1.0 CA A:GLY494 4.1 24.5 1.0 CB A:VAL493 4.2 28.8 1.0 CZ B:ARG233 4.2 20.9 1.0 C B:TYR229 4.4 15.1 1.0 O B:TYR229 4.5 14.6 1.0 NE B:ARG233 4.5 19.9 1.0 N A:VAL493 4.6 26.0 1.0 CG B:LEU230 4.7 19.0 1.0 CB B:TYR229 4.8 15.0 1.0 C A:SER492 4.8 25.1 1.0 CG2 A:VAL493 4.9 29.1 1.0 CG B:ARG233 4.9 18.5 1.0 C B:LEU230 5.0 15.9 1.0

Chlorine binding site 3 out of 5 in the Crystal Structure of Penicillin-Binding Protein 3 From Pseudomonas Aeruginosa in Complex with (5S)-Penicilloic Acid


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 Penicillin-Binding Protein 3 From Pseudomonas Aeruginosa in Complex with (5S)-Penicilloic Acid within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl602 b:32.6 occ:1.00 N B:VAL491 3.2 22.8 1.0 O B:HOH853 3.2 39.6 1.0 NH1 B:ARG504 3.3 18.9 1.0 O B:HOH750 3.6 29.2 1.0 CA B:LYS490 3.7 22.0 1.0 CB B:LYS490 3.8 22.4 1.0 NH2 B:ARG504 3.8 19.7 1.0 CB B:VAL491 3.9 24.8 1.0 CG B:LYS490 3.9 22.9 1.0 CG2 B:VAL491 3.9 25.0 1.0 C B:LYS490 4.0 22.5 1.0 CZ B:ARG504 4.0 18.8 1.0 CA B:VAL491 4.1 24.3 1.0 NZ B:LYS490 4.3 25.3 1.0 CE B:LYS490 4.5 24.7 1.0 O B:HOH746 4.5 18.1 1.0 O B:VAL491 4.5 24.6 1.0 CD B:LYS490 4.8 23.7 1.0 C B:VAL491 4.8 25.2 1.0 O B:HOH748 4.9 26.2 1.0

Chlorine binding site 4 out of 5 in the Crystal Structure of Penicillin-Binding Protein 3 From Pseudomonas Aeruginosa in Complex with (5S)-Penicilloic Acid


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 Penicillin-Binding Protein 3 From Pseudomonas Aeruginosa in Complex with (5S)-Penicilloic Acid within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl603 b:40.4 occ:1.00 N B:ASN501 3.3 33.7 1.0 NE B:ARG499 3.5 32.6 1.0 NH1 B:ARG499 3.7 33.2 1.0 CB B:ARG499 3.8 31.1 1.0 C B:ASN501 3.8 30.3 1.0 CA B:ASN501 3.8 33.7 1.0 N B:ALA502 4.0 27.3 1.0 N B:GLU500 4.0 33.5 1.0 CB B:ASN501 4.0 37.2 1.0 CZ B:ARG499 4.0 33.2 1.0 CB B:ALA502 4.2 24.7 1.0 O B:ASN501 4.3 30.4 1.0 C B:GLU500 4.4 34.7 1.0 CG B:ARG499 4.4 31.8 1.0 C B:ARG499 4.5 30.9 1.0 CA B:ARG499 4.5 30.7 1.0 CD B:ARG499 4.5 31.5 1.0 CA B:GLU500 4.6 36.7 1.0 CA B:ALA502 4.7 24.9 1.0 OD1 B:ASN501 4.7 45.0 1.0 CG B:ASN501 4.8 40.4 1.0 CB B:GLU500 4.9 41.3 1.0

Chlorine binding site 5 out of 5 in the Crystal Structure of Penicillin-Binding Protein 3 From Pseudomonas Aeruginosa in Complex with (5S)-Penicilloic Acid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Crystal Structure of Penicillin-Binding Protein 3 From Pseudomonas Aeruginosa in Complex with (5S)-Penicilloic Acid within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl604 b:45.6 occ:1.00 N B:GLY494 3.1 28.3 1.0 CA B:VAL493 3.5 31.6 1.0 CG1 B:VAL493 3.6 34.0 1.0 C B:VAL493 3.7 30.8 1.0 O B:SER492 4.1 28.0 1.0 CA B:GLY494 4.1 28.4 1.0 CB B:VAL493 4.1 33.5 1.0 N B:VAL493 4.6 30.5 1.0 C B:SER492 4.8 29.5 1.0 CG2 B:VAL493 4.8 33.4 1.0 O B:VAL493 5.0 31.8 1.0

S.S.Van Berkel, J.E.Nettleship, I.K.Leung, J.Brem, H.Choi, D.I.Stuart, T.D.Claridge, M.A.Mcdonough, R.J.Owens, J.Ren, C.J.Schofield. Binding of (5S)-Penicilloic Acid to Penicillin Binding Protein 3. Acs Chem.Biol. V. 8 2112 2013.
ISSN: ISSN 1554-8929
PubMed: 23899657
DOI: 10.1021/CB400200H