Zinc in PDB 2hb9: Crystal Structure of the Zinc-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (Inhibitor 3)

All present enzymatic activity of Crystal Structure of the Zinc-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (Inhibitor 3):
3.5.2.6;

The structure of Crystal Structure of the Zinc-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (Inhibitor 3), PDB code: 2hb9 was solved by L.Nauton, G.Garau, R.Kahn, O.Dideberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.67 / 1.75
Space group	P 64 2 2
Cell size a, b, c (Å), α, β, γ (°)	104.090, 104.090, 98.210, 90.00, 90.00, 120.00
R / Rfree (%)	17 / 19.1

The binding sites of Zinc atom in the Crystal Structure of the Zinc-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (Inhibitor 3) (pdb code 2hb9). 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 Zinc-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (Inhibitor 3), PDB code: 2hb9:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the Zinc-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (Inhibitor 3)


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 Zinc-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (Inhibitor 3) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:14.1 occ:1.00 N2 A:L13500 1.8 22.1 1.0 NE2 A:HIS196 2.1 14.3 1.0 NE2 A:HIS116 2.1 10.6 1.0 ND1 A:HIS118 2.1 9.7 1.0 C1 A:L13500 2.8 22.5 1.0 CD2 A:HIS116 2.9 7.5 1.0 CD2 A:HIS196 2.9 11.5 1.0 N3 A:L13500 3.0 24.4 1.0 CE1 A:HIS116 3.0 10.5 1.0 CG A:HIS118 3.1 10.9 1.0 CE1 A:HIS118 3.1 10.2 1.0 CE1 A:HIS196 3.1 12.4 1.0 S6 A:L13500 3.3 17.9 1.0 CB A:HIS118 3.4 9.4 1.0 N5 A:L13500 4.0 25.0 1.0 CG A:HIS116 4.0 10.4 1.0 ND1 A:HIS116 4.1 10.8 1.0 C4 A:L13500 4.1 26.7 1.0 CG A:HIS196 4.1 11.9 1.0 NE2 A:HIS118 4.2 11.1 1.0 ND1 A:HIS196 4.2 13.0 1.0 CD2 A:HIS118 4.2 9.9 1.0 OD1 A:ASP120 4.2 13.1 1.0 ZN A:ZN402 4.6 15.7 1.0 CD2 A:HIS121 4.6 12.2 1.0 CE2 A:PHE156 4.7 18.9 1.0 CA A:HIS118 4.8 10.6 1.0 CG2 A:THR197 4.9 10.7 1.0 OH A:TYR229 4.9 13.0 1.0 NE2 A:HIS121 5.0 13.3 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the Zinc-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (Inhibitor 3)


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 Zinc-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (Inhibitor 3) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:15.7 occ:1.00 OD2 A:ASP120 1.9 16.0 1.0 NE2 A:HIS121 2.0 13.3 1.0 NE2 A:HIS263 2.0 15.2 1.0 S6 A:L13500 2.3 17.9 1.0 CG A:ASP120 2.8 13.1 1.0 CE1 A:HIS121 2.9 12.2 1.0 C1 A:L13500 2.9 22.5 1.0 CD2 A:HIS263 3.0 15.7 1.0 CE1 A:HIS263 3.0 14.9 1.0 CD2 A:HIS121 3.0 12.2 1.0 OD1 A:ASP120 3.1 13.1 1.0 N5 A:L13500 3.3 25.0 1.0 N14 A:L13500 3.3 26.1 1.0 N2 A:L13500 3.9 22.1 1.0 ND1 A:HIS121 4.0 10.1 1.0 CG A:HIS121 4.1 12.3 1.0 ND1 A:HIS263 4.1 14.3 1.0 CB A:ASP120 4.1 12.7 1.0 CG A:HIS263 4.1 13.6 1.0 C4 A:L13500 4.4 26.7 1.0 CE1 A:HIS116 4.4 10.5 1.0 ZN A:ZN401 4.6 14.1 1.0 NE2 A:HIS116 4.6 10.6 1.0 N3 A:L13500 4.7 24.4 1.0 CZ3 A:TRP39 4.9 16.8 1.0 CD2 A:LEU69 4.9 12.3 1.0 CH2 A:TRP39 4.9 18.3 1.0 O A:ASP120 4.9 12.2 1.0 C A:ASP120 5.0 12.2 1.0

L.Nauton, R.Kahn, G.Garau, J.F.Hernandez, O.Dideberg. Structural Insights Into the Design of Inhibitors For the L1 Metallo-Beta-Lactamase From Stenotrophomonas Maltophilia. J.Mol.Biol. V. 375 257 2008.
ISSN: ISSN 0022-2836
PubMed: 17999929
DOI: 10.1016/J.JMB.2007.10.036