Calcium in PDB 4ax1: Q157N Mutant. Crystal Structure of the Mobile Metallo-Beta-Lactamase Aim-1 From Pseudomonas Aeruginosa: Insights Into Antibiotic Binding and the Role of GLN157

The structure of Q157N Mutant. Crystal Structure of the Mobile Metallo-Beta-Lactamase Aim-1 From Pseudomonas Aeruginosa: Insights Into Antibiotic Binding and the Role of GLN157, PDB code: 4ax1 was solved by H.-K.S.Leiros, P.S.Borra, B.O.Brandsdal, K.S.W.Edvardsen, J.Spencer, T.R.Walsh, O.Samuelsen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 1.40
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	77.992, 77.992, 239.766, 90.00, 90.00, 120.00
R / Rfree (%)	13 / 15

The structure of Q157N Mutant. Crystal Structure of the Mobile Metallo-Beta-Lactamase Aim-1 From Pseudomonas Aeruginosa: Insights Into Antibiotic Binding and the Role of GLN157 also contains other interesting chemical elements:

Magnesium	(Mg)	2 atoms
Zinc	(Zn)	2 atoms

The binding sites of Calcium atom in the Q157N Mutant. Crystal Structure of the Mobile Metallo-Beta-Lactamase Aim-1 From Pseudomonas Aeruginosa: Insights Into Antibiotic Binding and the Role of GLN157 (pdb code 4ax1). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Q157N Mutant. Crystal Structure of the Mobile Metallo-Beta-Lactamase Aim-1 From Pseudomonas Aeruginosa: Insights Into Antibiotic Binding and the Role of GLN157, PDB code: 4ax1:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Q157N Mutant. Crystal Structure of the Mobile Metallo-Beta-Lactamase Aim-1 From Pseudomonas Aeruginosa: Insights Into Antibiotic Binding and the Role of GLN157


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Q157N Mutant. Crystal Structure of the Mobile Metallo-Beta-Lactamase Aim-1 From Pseudomonas Aeruginosa: Insights Into Antibiotic Binding and the Role of GLN157 within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca3230 b:14.2 occ:0.85 O B:HOH2409 2.9 16.7 1.0 OG B:SER221 3.0 10.7 1.0 N B:HIS263 3.2 7.6 1.0 O B:HOH2291 3.6 11.6 1.0 CD B:PRO262 3.6 9.1 1.0 N B:PRO262 3.7 7.7 1.0 CA B:SER221 3.7 9.0 1.0 CB B:SER221 3.7 9.4 1.0 CB B:HIS263 3.8 9.8 1.0 CD2 B:HIS263 3.8 9.9 1.0 CB B:ALA266 3.8 12.1 1.0 CB B:THR261 3.8 8.4 1.0 OH B:TYR293 3.9 11.3 1.0 O B:HIS263 4.0 9.9 1.0 CA B:HIS263 4.0 8.3 1.0 CB B:PRO262 4.1 8.8 1.0 CG B:HIS263 4.1 10.3 1.0 C B:PRO262 4.2 8.4 1.0 CA B:PRO262 4.2 8.2 1.0 N B:SER221 4.2 9.6 1.0 CG B:PRO262 4.3 9.4 1.0 C B:THR261 4.3 8.4 1.0 OG1 B:THR261 4.4 10.5 1.0 C B:HIS263 4.5 9.2 1.0 CA B:THR261 4.6 8.3 1.0 CG2 B:THR261 4.6 9.8 1.0 O B:HOH2150 4.7 14.1 1.0 O B:HOH2293 4.8 17.9 1.0 C B:ASP220 4.9 9.2 1.0 CZ B:TYR293 5.0 9.2 1.0

Calcium binding site 2 out of 2 in the Q157N Mutant. Crystal Structure of the Mobile Metallo-Beta-Lactamase Aim-1 From Pseudomonas Aeruginosa: Insights Into Antibiotic Binding and the Role of GLN157


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Q157N Mutant. Crystal Structure of the Mobile Metallo-Beta-Lactamase Aim-1 From Pseudomonas Aeruginosa: Insights Into Antibiotic Binding and the Role of GLN157 within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca3234 b:17.4 occ:0.50 O B:HOH2343 2.4 26.6 1.0 O B:HOH2339 2.4 18.7 1.0 O B:HOH2275 2.5 16.1 1.0 O B:HOH2277 2.5 22.3 1.0 OD2 B:ASP257 4.3 12.5 1.0 O B:HOH2274 4.5 43.9 1.0 NH2 B:ARG206 4.5 25.0 1.0 OD1 B:ASP257 4.5 16.2 1.0 OD2 B:ASP255 4.6 21.4 1.0 OD1 B:ASP255 4.6 21.7 1.0 NH1 B:ARG206 4.7 20.1 1.0 O B:HOH2340 4.7 22.0 1.0 CG B:ASP257 4.9 11.3 1.0

H.-K.S.Leiros, P.S.Borra, B.O.Brandsdal, K.S.W.Edvardsen, J.Spencer, T.R.Walsh, O.Samuelsen. Crystal Structure of the Mobile Metallo-Beta-Lactamase Aim-1 From Pseudomonas Aeruginosa: Insights Into Antibiotic Binding and the Role of GLN157 Antimicrob.Agents Chemother. V. 56 4341 2012.
ISSN: ISSN 0066-4804
PubMed: 22664968
DOI: 10.1128/AAC.00448-12