Zinc in PDB 1ko2: Vim-2, A Zn-Beta-Lactamase From Pseudomonas Aeruginosa with An Oxidized Cys (Cysteinesulfonic)

All present enzymatic activity of Vim-2, A Zn-Beta-Lactamase From Pseudomonas Aeruginosa with An Oxidized Cys (Cysteinesulfonic):
3.5.2.6;

The structure of Vim-2, A Zn-Beta-Lactamase From Pseudomonas Aeruginosa with An Oxidized Cys (Cysteinesulfonic), PDB code: 1ko2 was solved by I.Garcia-Saez, J.-D.Docquier, G.M.Rossolini, O.Dideberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	21.45 / 2.20
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	67.180, 78.030, 80.130, 90.00, 90.00, 90.00
R / Rfree (%)	20.9 / 25.1

The binding sites of Zinc atom in the Vim-2, A Zn-Beta-Lactamase From Pseudomonas Aeruginosa with An Oxidized Cys (Cysteinesulfonic) (pdb code 1ko2). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Vim-2, A Zn-Beta-Lactamase From Pseudomonas Aeruginosa with An Oxidized Cys (Cysteinesulfonic), PDB code: 1ko2:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Vim-2, A Zn-Beta-Lactamase From Pseudomonas Aeruginosa with An Oxidized Cys (Cysteinesulfonic)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Vim-2, A Zn-Beta-Lactamase From Pseudomonas Aeruginosa with An Oxidized Cys (Cysteinesulfonic) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn300 b:18.9 occ:1.00 ND1 A:HIS118 2.1 14.5 1.0 NE2 A:HIS196 2.2 12.9 1.0 NE2 A:HIS116 2.2 11.7 1.0 O A:HOH467 2.2 12.5 1.0 O A:HOH461 2.6 21.6 1.0 CG A:HIS118 3.0 14.9 1.0 CD2 A:HIS196 3.0 13.4 1.0 CE1 A:HIS116 3.1 11.8 1.0 CE1 A:HIS118 3.2 14.2 1.0 CD2 A:HIS116 3.2 11.8 1.0 CE1 A:HIS196 3.2 13.4 1.0 CB A:HIS118 3.3 15.1 1.0 OD2 A:OCS221 3.8 15.3 1.0 OD1 A:ASP120 4.0 15.5 1.0 CD2 A:HIS118 4.2 14.6 1.0 ND1 A:HIS116 4.2 12.0 1.0 CG A:HIS196 4.2 13.6 1.0 NE2 A:HIS118 4.2 14.0 1.0 ND1 A:HIS196 4.3 13.4 1.0 CG A:HIS116 4.3 12.1 1.0 OD1 A:OCS221 4.4 14.8 1.0 SG A:OCS221 4.5 16.3 1.0 CB A:OCS221 4.6 15.2 1.0 CA A:HIS118 4.7 16.0 1.0 CG A:ASP120 4.9 15.8 1.0 O A:HOH445 4.9 17.4 1.0 OD2 A:ASP120 4.9 16.0 1.0 O A:HOH507 4.9 43.1 1.0 ND2 A:ASN233 5.0 34.7 1.0

Zinc binding site 2 out of 2 in the Vim-2, A Zn-Beta-Lactamase From Pseudomonas Aeruginosa with An Oxidized Cys (Cysteinesulfonic)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Vim-2, A Zn-Beta-Lactamase From Pseudomonas Aeruginosa with An Oxidized Cys (Cysteinesulfonic) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:21.8 occ:1.00 NE2 A:HIS170 2.1 17.1 1.0 OXT A:ACT400 2.1 17.0 1.0 OXT A:ACT401 2.3 17.6 1.0 O A:ACT401 2.8 18.2 1.0 C A:ACT401 2.9 18.1 1.0 C A:ACT400 2.9 16.8 1.0 CE1 A:HIS170 3.1 17.5 1.0 O A:ACT400 3.1 16.6 1.0 CD2 A:HIS170 3.1 16.7 1.0 ND1 A:HIS170 4.2 17.3 1.0 CG A:HIS170 4.3 17.3 1.0 CB A:ALA135 4.3 15.4 1.0 CH3 A:ACT401 4.4 17.5 1.0 CH3 A:ACT400 4.4 16.3 1.0 CA A:ALA135 4.9 15.8 1.0

I.Garcia-Saez, J.-D.Docquier, G.M.Rossolini, O.Dideberg. The Three-Dimensional Structure of Vim-2, A Zn-Beta-Lactamase From Pseudomonas Aeruginosa in Its Reduced and Oxidised Form J.Mol.Biol. V. 375 604 2008.
ISSN: ISSN 0022-2836
PubMed: 18061205
DOI: 10.1016/J.JMB.2007.11.012