Zinc in PDB 2h6a: Crystal Structure of the Zinc-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (Mono Zinc Form)

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

The structure of Crystal Structure of the Zinc-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (Mono Zinc Form), PDB code: 2h6a 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)	19.74 / 1.80
Space group	P 62 2 2
Cell size a, b, c (Å), α, β, γ (°)	104.220, 104.220, 195.740, 90.00, 90.00, 120.00
R / Rfree (%)	17.2 / 21

The binding sites of Zinc atom in the Crystal Structure of the Zinc-Beta-Lactamase L1 From Stenotrophomonas Maltophilia (Mono Zinc Form) (pdb code 2h6a). 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 (Mono Zinc Form), PDB code: 2h6a:
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 (Mono Zinc Form)


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 (Mono Zinc Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn320 b:14.7 occ:1.00 NE2 A:HIS196 2.1 8.9 1.0 ND1 A:HIS118 2.1 7.9 1.0 NE2 A:HIS116 2.2 9.7 1.0 O A:HOH1308 2.4 16.8 1.0 O A:HOH1311 2.8 14.8 1.0 CD2 A:HIS196 2.9 8.1 1.0 CE1 A:HIS118 3.0 8.2 1.0 CE1 A:HIS116 3.1 7.5 1.0 CD2 A:HIS116 3.1 7.1 1.0 CE1 A:HIS196 3.1 7.8 1.0 CG A:HIS118 3.1 7.8 1.0 CB A:HIS118 3.5 7.4 1.0 O1 A:SO41106 3.7 35.5 1.0 O A:HOH1309 3.8 26.2 1.0 CG A:HIS196 4.1 8.1 1.0 ND1 A:HIS116 4.1 7.7 1.0 NE2 A:HIS118 4.2 6.5 1.0 CG A:HIS116 4.2 8.2 1.0 ND1 A:HIS196 4.2 9.3 1.0 OD1 A:ASP120 4.2 19.8 1.0 CD2 A:HIS118 4.2 7.8 1.0 CD2 A:HIS121 4.3 12.0 1.0 NE2 A:HIS121 4.4 14.2 1.0 O4 A:SO41106 4.6 32.9 1.0 O A:HOH1310 4.7 28.6 1.0 S A:SO41106 4.7 35.0 1.0 CE2 A:PHE156 4.9 19.6 1.0 CA A:HIS118 5.0 7.3 1.0

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


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 (Mono Zinc Form) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn321 b:16.4 occ:1.00 NE2 B:HIS116 2.1 9.2 1.0 NE2 B:HIS196 2.1 11.9 1.0 ND1 B:HIS118 2.1 7.9 1.0 O B:HOH1296 2.5 16.9 1.0 CD2 B:HIS196 2.9 11.7 1.0 O B:HOH1313 3.0 16.7 1.0 CE1 B:HIS118 3.0 7.5 1.0 CD2 B:HIS116 3.0 8.8 1.0 CE1 B:HIS116 3.0 10.1 1.0 CG B:HIS118 3.2 7.6 1.0 CE1 B:HIS196 3.2 11.9 1.0 CB B:HIS118 3.6 7.5 1.0 O4 B:SO41105 3.7 38.6 1.0 O B:HOH1297 3.9 25.8 1.0 ND1 B:HIS116 4.1 9.2 1.0 CG B:HIS116 4.1 9.8 1.0 OD1 B:ASP120 4.1 20.7 1.0 CG B:HIS196 4.1 10.3 1.0 NE2 B:HIS118 4.2 8.2 1.0 ND1 B:HIS196 4.2 10.2 1.0 CD2 B:HIS118 4.3 6.8 1.0 CD2 B:HIS121 4.3 12.1 1.0 NE2 B:HIS121 4.3 11.2 1.0 O1 B:SO41105 4.5 37.5 1.0 S B:SO41105 4.7 39.0 1.0 CE2 B:PHE156 4.8 17.9 1.0 O B:HOH1347 4.9 32.0 1.0 O B:HOH1355 4.9 39.4 1.0 CA B:HIS118 5.0 7.9 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