Magnesium 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:

Calcium	(Ca)	2 atoms
Zinc	(Zn)	2 atoms

The binding sites of Magnesium 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 Magnesium atom.
In total 2 binding sites of Magnesium 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 Magnesium binding site number: 1; 2;

Magnesium 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 Magnesium with other atoms in the Mg 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:Mg3231 b:44.3 occ:1.00 O B:HOH2027 2.5 44.3 1.0 OD1 B:ASN98 2.6 16.1 1.0 O B:HOH2025 2.9 17.9 1.0 O B:HOH2410 3.0 30.6 1.0 ND2 B:ASN98 3.3 16.4 1.0 CG B:ASN98 3.3 13.4 1.0 O B:ALA42 3.6 17.3 1.0 O B:HOH2115 3.8 27.2 1.0 CB B:PRO41 4.1 22.8 1.0 O B:HOH2058 4.1 26.8 1.0 O B:GLN94 4.1 13.8 1.0 CB B:GLN94 4.2 16.2 1.0 OE1 B:GLN94 4.2 21.9 1.0 O B:HOH2001 4.4 49.4 1.0 CG B:GLN94 4.4 17.7 1.0 N B:ALA42 4.4 17.1 1.0 CA B:GLN94 4.5 14.7 1.0 C B:ALA42 4.5 15.5 1.0 CA B:PRO41 4.7 19.1 1.0 C B:GLN94 4.7 12.8 1.0 CD B:GLN94 4.7 18.6 1.0 CB B:ASN98 4.7 10.8 1.0 C B:PRO41 5.0 19.2 1.0

Magnesium 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 Magnesium with other atoms in the Mg 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:Mg3232 b:37.5 occ:0.80 O B:HOH2370 2.7 17.6 1.0 O B:HOH2347 2.8 37.2 1.0 O B:ALA266 3.1 14.8 1.0 O B:HOH2372 3.3 58.5 1.0 O B:HOH2346 3.4 29.7 1.0 CA B:TYR293 3.7 9.2 1.0 CD1 B:TYR293 3.8 10.5 1.0 CB B:TYR293 3.9 10.3 1.0 N B:TYR293 4.2 10.6 1.0 C B:ALA266 4.2 12.1 1.0 CA B:SER267 4.3 11.5 1.0 CG B:TYR293 4.3 8.7 1.0 O B:HOH2348 4.5 18.6 1.0 O B:HOH2375 4.6 19.0 1.0 C B:ARG292 4.7 11.1 1.0 N B:SER267 4.7 10.9 1.0 O B:ARG292 4.8 11.5 1.0 NH1 B:ARG292 4.8 26.1 1.0 O B:ALA289 4.8 12.0 1.0 CE1 B:TYR293 4.9 11.0 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