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

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

The structure of Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with Hydrolyzed Imipnem, PDB code: 6uaf 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)	34.31 / 1.90
Space group	P 64 2 2
Cell size a, b, c (Å), α, β, γ (°)	104.835, 104.835, 98.627, 90.00, 90.00, 120.00
R / Rfree (%)	17.2 / 20.8

The binding sites of Zinc atom in the Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with Hydrolyzed Imipnem (pdb code 6uaf). 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 Imipnem, PDB code: 6uaf:
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 Imipnem


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 Imipnem within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:24.1 occ:1.00 OD2 A:ASP109 2.1 18.6 1.0 O A:HOH408 2.1 78.0 1.0 NE2 A:HIS246 2.1 23.3 1.0 NE2 A:HIS110 2.2 22.9 1.0 N4 A:HIW301 2.2 34.3 1.0 O32 A:HIW301 2.4 35.4 1.0 CG A:ASP109 3.0 19.5 1.0 C3 A:HIW301 3.0 40.2 1.0 CE1 A:HIS110 3.1 22.1 1.0 C31 A:HIW301 3.1 41.4 1.0 CD2 A:HIS246 3.1 23.5 1.0 CE1 A:HIS246 3.1 24.4 1.0 CD2 A:HIS110 3.2 18.2 1.0 OD1 A:ASP109 3.3 18.4 1.0 C5 A:HIW301 3.4 34.2 1.0 ZN A:ZN303 3.6 30.0 1.0 C6 A:HIW301 3.8 30.6 1.0 O62 A:HIW301 3.9 26.1 1.0 ND1 A:HIS110 4.2 15.2 1.0 ND1 A:HIS246 4.2 21.4 1.0 CG A:HIS246 4.3 19.1 1.0 CG A:HIS110 4.3 18.4 1.0 O31 A:HIW301 4.3 38.2 1.0 CB A:ASP109 4.3 18.6 1.0 C2 A:HIW301 4.4 42.4 1.0 C61 A:HIW301 4.4 32.3 1.0 NE2 A:HIS105 4.5 22.9 1.0 CE1 A:HIS105 4.5 18.0 1.0 C1 A:HIW301 4.6 34.9 1.0 OG A:SER206 4.6 17.1 1.0 NE2 A:HIS181 4.7 22.9 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 Imipnem


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 Imipnem within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn303 b:30.0 occ:1.00 O A:HOH408 1.9 78.0 1.0 NE2 A:HIS105 2.0 22.9 1.0 ND1 A:HIS107 2.2 23.9 1.0 NE2 A:HIS181 2.2 22.9 1.0 CD2 A:HIS181 2.9 16.5 1.0 CE1 A:HIS105 3.0 18.0 1.0 CD2 A:HIS105 3.0 20.1 1.0 CG A:HIS107 3.1 21.2 1.0 CE1 A:HIS107 3.2 23.8 1.0 CE1 A:HIS181 3.3 20.9 1.0 CB A:HIS107 3.3 17.3 1.0 O62 A:HIW301 3.4 26.1 1.0 O32 A:HIW301 3.5 35.4 1.0 ZN A:ZN302 3.6 24.1 1.0 CD2 A:HIS110 3.9 18.2 1.0 OD1 A:ASP109 4.0 18.4 1.0 ND1 A:HIS105 4.1 22.2 1.0 NE2 A:HIS110 4.1 22.9 1.0 CG A:HIS105 4.1 22.9 1.0 CG A:HIS181 4.2 17.1 1.0 C31 A:HIW301 4.2 41.4 1.0 CD2 A:HIS107 4.3 21.1 1.0 NE2 A:HIS107 4.3 18.2 1.0 ND1 A:HIS181 4.3 17.5 1.0 N4 A:HIW301 4.4 34.3 1.0 C3 A:HIW301 4.6 40.2 1.0 C61 A:HIW301 4.7 32.3 1.0 OD2 A:ASP109 4.8 18.6 1.0 CA A:HIS107 4.8 17.9 1.0 CG A:ASP109 4.8 19.5 1.0 C62 A:HIW301 4.9 29.2 1.0 CG2 A:THR182 5.0 15.1 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 Imipnem To Be Published.