Zinc in PDB 1sml: Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia

All present enzymatic activity of Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia:
3.5.2.6;

The structure of Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia, PDB code: 1sml was solved by J.H.Ullah, T.R.Walsh, I.A.Taylor, D.C.Emery, C.S.Verma, S.J.Gamblin, J.Spencer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.70
Space group	P 64 2 2
Cell size a, b, c (Å), α, β, γ (°)	105.230, 105.230, 97.720, 90.00, 90.00, 120.00
R / Rfree (%)	18 / 23.3

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

Zinc binding site 1 out of 2 in the Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn270 b:17.0 occ:1.00 NE2 A:HIS89 2.0 14.4 1.0 O A:HOH568 2.1 17.6 1.0 OD2 A:ASP88 2.1 15.3 1.0 NE2 A:HIS225 2.1 13.7 1.0 O A:HOH528 2.4 21.0 1.0 CE1 A:HIS89 2.9 17.0 1.0 CG A:ASP88 2.9 17.2 1.0 CE1 A:HIS225 3.0 13.9 1.0 CD2 A:HIS225 3.0 18.6 1.0 CD2 A:HIS89 3.1 14.3 1.0 OD1 A:ASP88 3.2 16.2 1.0 ZN A:ZN271 3.5 17.1 1.0 O A:HOH463 3.8 28.7 1.0 ND1 A:HIS89 4.1 14.9 1.0 NE2 A:HIS84 4.1 14.4 1.0 ND1 A:HIS225 4.1 16.4 1.0 O A:HOH451 4.1 30.4 1.0 CE1 A:HIS84 4.1 14.9 1.0 CG A:HIS225 4.1 17.4 1.0 CG A:HIS89 4.2 16.9 1.0 CB A:ASP88 4.3 13.3 1.0 OG A:SER185 4.6 19.0 1.0 NE2 A:HIS160 4.7 14.5 1.0 O A:HOH285 4.7 48.2 1.0

Zinc binding site 2 out of 2 in the Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Metallo Beta Lactamase L1 From Stenotrophomonas Maltophilia within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn271 b:17.1 occ:1.00 O A:HOH568 1.9 17.6 1.0 NE2 A:HIS84 2.0 14.4 1.0 NE2 A:HIS160 2.0 14.5 1.0 ND1 A:HIS86 2.1 15.5 1.0 CD2 A:HIS160 2.9 15.2 1.0 CD2 A:HIS84 3.0 14.8 1.0 CE1 A:HIS86 3.0 14.6 1.0 CE1 A:HIS84 3.0 14.9 1.0 O A:HOH528 3.0 21.0 1.0 CE1 A:HIS160 3.1 15.9 1.0 CG A:HIS86 3.2 15.4 1.0 O A:HOH463 3.4 28.7 1.0 ZN A:ZN270 3.5 17.0 1.0 CB A:HIS86 3.5 16.8 1.0 OD1 A:ASP88 4.1 16.2 1.0 ND1 A:HIS84 4.1 16.1 1.0 CG A:HIS84 4.1 13.9 1.0 CG A:HIS160 4.1 15.8 1.0 NE2 A:HIS89 4.1 14.4 1.0 CD2 A:HIS89 4.1 14.3 1.0 ND1 A:HIS160 4.1 15.2 1.0 NE2 A:HIS86 4.1 13.4 1.0 CD2 A:HIS86 4.2 12.8 1.0 OD2 A:ASP88 4.7 15.3 1.0 CG A:ASP88 4.8 17.2 1.0 CA A:HIS86 4.9 14.6 1.0 CE2 A:PHE124 4.9 21.3 1.0 O A:HOH451 5.0 30.4 1.0 CG2 A:THR161 5.0 15.4 1.0

J.H.Ullah, T.R.Walsh, I.A.Taylor, D.C.Emery, C.S.Verma, S.J.Gamblin, J.Spencer. The Crystal Structure of the L1 Metallo-Beta-Lactamase From Stenotrophomonas Maltophilia at 1.7 A Resolution. J.Mol.Biol. V. 284 125 1998.
ISSN: ISSN 0022-2836
PubMed: 9811546
DOI: 10.1006/JMBI.1998.2148