Zinc in PDB 6uah: Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with Hydrolyzed Meropenem

All present enzymatic activity of Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with Hydrolyzed Meropenem:
3.5.2.6;

The structure of Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with Hydrolyzed Meropenem, PDB code: 6uah was solved by Y.Kim, N.Maltseva, M.Endres, A.Joachimiak, Center For Structural Genomicsof Infectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.89 / 1.98
Space group	P 64 2 2
Cell size a, b, c (Å), α, β, γ (°)	104.410, 104.410, 98.849, 90.00, 90.00, 120.00
R / Rfree (%)	17.3 / 20.3

The binding sites of Zinc atom in the Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with Hydrolyzed Meropenem (pdb code 6uah). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with Hydrolyzed Meropenem, PDB code: 6uah:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with Hydrolyzed Meropenem


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 Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with Hydrolyzed Meropenem within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:26.1 occ:1.00 O71 A:LMP303 2.0 29.7 1.0 NE2 A:HIS181 2.0 30.1 1.0 NE2 A:HIS105 2.1 22.4 1.0 ND1 A:HIS107 2.1 23.4 1.0 C7 A:LMP303 2.7 30.5 1.0 O72 A:LMP303 2.8 26.9 1.0 CD2 A:HIS181 2.9 23.2 1.0 CD2 A:HIS105 3.0 22.8 1.0 CE1 A:HIS105 3.1 23.4 1.0 CE1 A:HIS181 3.1 24.1 1.0 CE1 A:HIS107 3.1 24.7 1.0 CG A:HIS107 3.1 24.9 1.0 CB A:HIS107 3.4 22.6 1.0 O32 A:LMP303 3.8 30.1 1.0 CG A:HIS105 4.1 23.5 1.0 CG A:HIS181 4.1 25.4 1.0 ND1 A:HIS105 4.1 24.4 1.0 ZN A:ZN302 4.1 29.4 1.0 ND1 A:HIS181 4.1 22.3 1.0 NE2 A:HIS107 4.2 22.2 1.0 C6 A:LMP303 4.2 31.5 1.0 CD2 A:HIS107 4.3 19.5 1.0 CD2 A:HIS110 4.3 22.9 1.0 C31 A:LMP303 4.3 32.0 1.0 N4 A:LMP303 4.4 27.7 1.0 OD1 A:ASP109 4.4 26.8 1.0 NE2 A:HIS110 4.6 26.4 1.0 C3 A:LMP303 4.6 27.4 1.0 C62 A:LMP303 4.7 34.7 1.0 C61 A:LMP303 4.8 38.2 1.0 CA A:HIS107 4.9 23.1 1.0 C5 A:LMP303 4.9 31.2 1.0 CG2 A:THR182 5.0 16.9 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with Hydrolyzed Meropenem


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 Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with Hydrolyzed Meropenem within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:29.4 occ:1.00 N4 A:LMP303 2.0 27.7 1.0 OD2 A:ASP109 2.1 28.3 1.0 NE2 A:HIS110 2.1 26.4 1.0 NE2 A:HIS246 2.1 26.4 1.0 O32 A:LMP303 2.4 30.1 1.0 O71 A:LMP303 2.8 29.7 1.0 C3 A:LMP303 2.9 27.4 1.0 CG A:ASP109 3.0 29.7 1.0 C31 A:LMP303 3.0 32.0 1.0 CD2 A:HIS246 3.0 26.0 1.0 CE1 A:HIS110 3.0 24.3 1.0 CD2 A:HIS110 3.1 22.9 1.0 CE1 A:HIS246 3.2 30.4 1.0 OD1 A:ASP109 3.2 26.8 1.0 C5 A:LMP303 3.3 31.2 1.0 C7 A:LMP303 3.6 30.5 1.0 C6 A:LMP303 3.8 31.5 1.0 C61 A:LMP303 4.1 38.2 1.0 C2 A:LMP303 4.1 32.8 1.0 ZN A:ZN301 4.1 26.1 1.0 ND1 A:HIS110 4.2 20.6 1.0 CG A:HIS110 4.2 25.4 1.0 CG A:HIS246 4.2 24.1 1.0 O31 A:LMP303 4.2 25.7 1.0 ND1 A:HIS246 4.2 23.8 1.0 C1 A:LMP303 4.3 27.4 1.0 CB A:ASP109 4.3 27.5 1.0 O72 A:LMP303 4.6 26.9 1.0 NE2 A:HIS105 4.6 22.4 1.0 CE1 A:HIS105 4.6 23.4 1.0 OG A:SER206 4.7 24.8 1.0 CH2 A:TRP38 4.8 59.3 1.0 CZ3 A:TRP38 4.8 36.3 1.0 O62 A:LMP303 5.0 37.9 1.0

Y.Kim, N.Maltseva, M.Endres, A.Joachimiak, Center For Structural Genomics Of Infectious Diseases(Csgid). Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with Hydrolyzed Meropenem To Be Published.