Chlorine in PDB 2fhx: Pseudomonas Aeruginosa Spm-1 Metallo-Beta-Lactamase

All present enzymatic activity of Pseudomonas Aeruginosa Spm-1 Metallo-Beta-Lactamase:
3.5.2.6;

The structure of Pseudomonas Aeruginosa Spm-1 Metallo-Beta-Lactamase, PDB code: 2fhx was solved by T.A.Murphy, L.E.Catto, S.E.Halford, A.T.Hadfield, W.Minor, T.R.Walsh, J.Spencer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.90
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	126.936, 126.936, 90.461, 90.00, 90.00, 120.00
R / Rfree (%)	19.4 / 24.7

The structure of Pseudomonas Aeruginosa Spm-1 Metallo-Beta-Lactamase also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Chlorine atom in the Pseudomonas Aeruginosa Spm-1 Metallo-Beta-Lactamase (pdb code 2fhx). 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 Pseudomonas Aeruginosa Spm-1 Metallo-Beta-Lactamase, PDB code: 2fhx:

Chlorine binding site 1 out of 1 in the Pseudomonas Aeruginosa Spm-1 Metallo-Beta-Lactamase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Pseudomonas Aeruginosa Spm-1 Metallo-Beta-Lactamase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl601 b:50.4 occ:1.00 O B:HOH653 3.0 39.3 1.0 ND1 B:HIS164 3.5 35.2 1.0 CD B:ARG150D 3.6 32.0 0.5 NH1 B:ARG150D 3.6 31.8 0.5 O B:HOH679 3.8 41.7 1.0 CG B:ARG150D 4.1 32.2 0.5 O B:HOH729 4.2 41.2 1.0 CE1 B:HIS164 4.3 36.0 1.0 CB B:ASN149 4.4 30.9 1.0 CG B:HIS164 4.5 35.5 1.0 NE B:ARG150D 4.5 32.1 0.5 CZ B:ARG150D 4.5 31.9 0.5 ND2 B:ASN149 4.6 28.5 1.0 CB B:HIS164 4.7 35.2 1.0 O B:HOH645 4.7 33.5 1.0 CG B:ASN149 4.8 30.6 1.0 O B:LEU161 5.0 37.8 1.0

T.A.Murphy, L.E.Catto, S.E.Halford, A.T.Hadfield, W.Minor, T.R.Walsh, J.Spencer. Crystal Structure of Pseudomonas Aeruginosa Spm-1 Provides Insights Into Variable Zinc Affinity of Metallo-Beta-Lactamases. J.Mol.Biol. V. 357 890 2006.
ISSN: ISSN 0022-2836
PubMed: 16460758
DOI: 10.1016/J.JMB.2006.01.003