Zinc in PDB 6u10: Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with the Inhibitor Captopril

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

The structure of Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with the Inhibitor Captopril, PDB code: 6u10 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)	46.22 / 1.40
Space group	P 64 2 2
Cell size a, b, c (Å), α, β, γ (°)	104.537, 104.537, 98.723, 90.00, 90.00, 120.00
R / Rfree (%)	14.5 / 16.7

The binding sites of Zinc atom in the Crystal Structure of the Metallo-Beta-Lactamase L1 From Stenotrophomonas Maltophilia in the Complex with the Inhibitor Captopril (pdb code 6u10). 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 the Inhibitor Captopril, PDB code: 6u10:
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 the Inhibitor Captopril


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 the Inhibitor Captopril within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:19.5 occ:1.00 OD2 A:ASP109 2.0 19.3 1.0 NE2 A:HIS110 2.0 18.2 1.0 NE2 A:HIS246 2.0 18.8 1.0 S A:X8Z303 2.3 21.1 0.5 S A:X8Z303 2.3 21.0 0.5 CG A:ASP109 2.7 18.5 1.0 OD1 A:ASP109 2.9 18.2 1.0 CE1 A:HIS110 2.9 18.9 1.0 CE1 A:HIS246 3.0 19.5 1.0 CD2 A:HIS110 3.0 19.0 1.0 CD2 A:HIS246 3.1 19.6 1.0 C1 A:X8Z303 3.3 26.8 0.3 C1 A:X8Z303 3.4 27.8 0.3 O2 A:FMT304 3.4 42.0 1.0 ZN A:ZN302 3.8 19.5 1.0 C3 A:X8Z303 3.9 33.1 0.3 ND1 A:HIS110 4.0 17.8 1.0 ND1 A:HIS246 4.1 19.2 1.0 CG A:HIS110 4.1 17.4 1.0 C3 A:X8Z303 4.1 34.0 0.3 C A:FMT304 4.1 42.9 1.0 CB A:ASP109 4.1 18.3 1.0 CG A:HIS246 4.2 19.2 1.0 C2 A:X8Z303 4.2 32.8 0.3 NE2 A:HIS105 4.3 16.7 1.0 C2 A:X8Z303 4.3 33.9 0.3 CE1 A:HIS105 4.4 16.9 1.0 OG A:SER206 5.0 22.1 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 the Inhibitor Captopril


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 the Inhibitor Captopril within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:19.5 occ:1.00 NE2 A:HIS181 2.0 17.9 1.0 NE2 A:HIS105 2.1 16.7 1.0 ND1 A:HIS107 2.1 17.0 1.0 S A:X8Z303 2.2 21.1 0.5 S A:X8Z303 2.3 21.0 0.5 CD2 A:HIS181 2.9 17.5 1.0 CD2 A:HIS105 2.9 16.1 1.0 CE1 A:HIS107 3.0 17.6 1.0 CE1 A:HIS105 3.0 16.9 1.0 CE1 A:HIS181 3.1 18.4 1.0 CG A:HIS107 3.1 17.3 1.0 C1 A:X8Z303 3.3 27.8 0.3 C1 A:X8Z303 3.4 26.8 0.3 CB A:HIS107 3.5 16.8 1.0 O2 A:FMT304 3.7 42.0 1.0 ZN A:ZN301 3.8 19.5 1.0 ND1 A:HIS105 4.1 17.8 1.0 CG A:HIS105 4.1 17.1 1.0 NE2 A:HIS107 4.1 17.8 1.0 CG A:HIS181 4.1 16.5 1.0 ND1 A:HIS181 4.2 18.5 1.0 CD2 A:HIS107 4.2 17.9 1.0 CD2 A:HIS110 4.2 19.0 1.0 OD1 A:ASP109 4.4 18.2 1.0 NE2 A:HIS110 4.4 18.2 1.0 C2 A:X8Z303 4.4 33.9 0.3 C2 A:X8Z303 4.6 32.8 0.3 C A:FMT304 4.9 42.9 1.0 CA A:HIS107 5.0 17.0 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 the Inhibitor Captopril. To Be Published.