Zinc in PDB 4awy: 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 Crystal Structure of the Mobile Metallo-Beta-Lactamase Aim-1 From Pseudomonas Aeruginosa: Insights Into Antibiotic Binding and the Role of GLN157, PDB code: 4awy 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)	20.00 / 1.60
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	77.831, 77.831, 239.018, 90.00, 90.00, 120.00
R / Rfree (%)	12.9 / 15.8

The structure of 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)	4 atoms
Calcium	(Ca)	1 atom

The binding sites of Zinc atom in the Crystal Structure of the Mobile Metallo-Beta-Lactamase Aim-1 From Pseudomonas Aeruginosa: Insights Into Antibiotic Binding and the Role of GLN157 (pdb code 4awy). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of the Mobile Metallo-Beta-Lactamase Aim-1 From Pseudomonas Aeruginosa: Insights Into Antibiotic Binding and the Role of GLN157, PDB code: 4awy:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the 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 Zinc with other atoms in the Zn binding site number 1 of 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:Zn3228 b:9.1 occ:1.00 O B:HOH2136 1.9 10.2 1.0 NE2 B:HIS196 2.0 7.6 1.0 NE2 B:HIS116 2.1 7.4 1.0 ND1 B:HIS118 2.1 8.1 1.0 CD2 B:HIS196 2.9 7.9 1.0 CD2 B:HIS116 3.0 7.7 1.0 CE1 B:HIS116 3.0 8.3 1.0 O B:HOH2157 3.0 11.6 1.0 CE1 B:HIS118 3.0 7.7 1.0 CE1 B:HIS196 3.1 8.6 1.0 CG B:HIS118 3.1 7.4 1.0 O B:HOH2212 3.4 22.6 1.0 ZN B:ZN3229 3.5 11.0 1.0 CB B:HIS118 3.5 8.3 1.0 CD2 B:HIS121 4.1 8.4 1.0 ND1 B:HIS116 4.1 8.5 1.0 CG B:HIS196 4.1 7.8 1.0 OD1 B:ASP120 4.1 10.1 1.0 CG B:HIS116 4.1 7.9 1.0 ND1 B:HIS196 4.2 8.5 1.0 NE2 B:HIS118 4.2 8.3 1.0 NE2 B:HIS121 4.2 6.9 1.0 CD2 B:HIS118 4.2 10.0 1.0 OE1 B:GLN157 4.3 14.1 1.0 O B:HOH2154 4.6 25.1 1.0 OD2 B:ASP120 4.8 10.1 1.0 OG B:SER221 4.8 8.5 1.0 CG2 B:THR197 4.9 9.9 1.0 CG B:ASP120 4.9 8.3 1.0 CB B:SER221 4.9 7.3 1.0 CA B:HIS118 4.9 8.7 1.0 O B:HOH2282 4.9 14.0 1.0

Zinc binding site 2 out of 3 in the 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 Zinc with other atoms in the Zn binding site number 2 of 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:Zn3229 b:11.0 occ:1.00 O B:HOH2136 2.0 10.2 1.0 NE2 B:HIS263 2.0 8.3 1.0 NE2 B:HIS121 2.1 6.9 1.0 OD2 B:ASP120 2.1 10.1 1.0 O B:HOH2157 2.3 11.6 1.0 CD2 B:HIS263 3.0 8.6 1.0 CG B:ASP120 3.0 8.3 1.0 CE1 B:HIS263 3.0 10.4 1.0 CD2 B:HIS121 3.0 8.4 1.0 CE1 B:HIS121 3.0 8.1 1.0 OD1 B:ASP120 3.3 10.1 1.0 ZN B:ZN3228 3.5 9.1 1.0 O B:HOH2212 3.8 22.6 1.0 ND1 B:HIS263 4.1 9.6 1.0 ND1 B:HIS121 4.1 7.9 1.0 CG B:HIS263 4.1 8.1 1.0 NE2 B:HIS116 4.2 7.4 1.0 CG B:HIS121 4.2 7.0 1.0 O B:HOH2282 4.2 14.0 1.0 CE1 B:HIS116 4.3 8.3 1.0 CB B:ASP120 4.4 10.1 1.0 OG B:SER221 4.5 8.5 1.0 NE2 B:HIS196 4.7 7.6 1.0 O B:HOH2154 4.8 25.1 1.0 CD1 B:ILE68 4.9 11.2 1.0

Zinc binding site 3 out of 3 in the 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 Zinc with other atoms in the Zn binding site number 3 of 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:Zn3235 b:19.6 occ:0.45 O B:HOH2323 2.4 15.4 1.0 O B:HOH2260 2.4 14.2 1.0 O B:HOH2326 2.4 26.9 1.0 O B:HOH2262 2.5 18.1 1.0 O B:HOH2276 4.2 55.9 1.0 OD2 B:ASP257 4.2 9.8 1.0 NH2 B:ARG206 4.5 20.1 1.0 OD1 B:ASP257 4.5 13.2 1.0 OD2 B:ASP255 4.5 18.6 1.0 OD1 B:ASP255 4.5 18.5 1.0 NH1 B:ARG206 4.6 19.8 1.0 O B:HOH2321 4.7 19.6 1.0 CG B:ASP257 4.8 9.8 1.0 CG B:ASP255 5.0 13.6 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