Zinc in PDB 5act: W228S-Investigation of the Impact From Residues W228 and Y233 in the Metallo-Beta-Lactamase Gim-1

The structure of W228S-Investigation of the Impact From Residues W228 and Y233 in the Metallo-Beta-Lactamase Gim-1, PDB code: 5act was solved by S.Skagseth, T.J.Carlsen, G.E.K.Bjerga, J.Spencer, O.Samuelsen, H.-K.S.Leiros, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.82 / 1.81
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	38.644, 133.007, 40.860, 90.00, 95.28, 90.00
R / Rfree (%)	17.9 / 23

The binding sites of Zinc atom in the W228S-Investigation of the Impact From Residues W228 and Y233 in the Metallo-Beta-Lactamase Gim-1 (pdb code 5act). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the W228S-Investigation of the Impact From Residues W228 and Y233 in the Metallo-Beta-Lactamase Gim-1, PDB code: 5act:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the W228S-Investigation of the Impact From Residues W228 and Y233 in the Metallo-Beta-Lactamase Gim-1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of W228S-Investigation of the Impact From Residues W228 and Y233 in the Metallo-Beta-Lactamase Gim-1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1297 b:29.3 occ:1.00 HE1 A:HIS196 1.1 26.8 1.0 OE2 B:GLU62 1.9 37.1 1.0 CE1 A:HIS196 2.0 22.3 1.0 ND1 A:HIS118 2.1 31.2 1.0 NE2 A:HIS116 2.1 26.0 1.0 CD B:GLU62 2.7 40.6 1.0 NE2 A:HIS196 2.8 27.0 1.0 HE2 A:HIS196 2.8 32.4 1.0 HB2 A:HIS118 2.8 41.8 1.0 OE1 B:GLU62 2.9 40.8 1.0 CG A:HIS118 3.0 28.0 1.0 CD2 A:HIS116 3.0 23.9 1.0 CE1 A:HIS118 3.1 28.8 1.0 ND1 A:HIS196 3.1 30.2 1.0 CE1 A:HIS116 3.1 31.5 1.0 HD2 A:HIS116 3.2 28.7 1.0 CB A:HIS118 3.3 34.8 1.0 HE1 A:HIS118 3.3 34.6 1.0 HB3 A:HIS118 3.3 41.8 1.0 HE1 A:HIS116 3.4 37.8 1.0 HD1 A:HIS196 3.4 36.2 1.0 HG21 A:THR197 3.9 28.3 1.0 HB2 A:OCS221 3.9 38.5 1.0 OD1 A:ASP120 4.0 28.7 0.5 CD2 A:HIS196 4.0 19.8 1.0 HG22 A:THR197 4.1 28.3 1.0 O A:HOH2056 4.1 46.5 1.0 OD2 A:OCS221 4.1 35.8 1.0 CD2 A:HIS118 4.2 31.7 1.0 NE2 A:HIS118 4.2 33.6 1.0 CG A:HIS196 4.2 23.6 1.0 CG B:GLU62 4.2 40.5 1.0 CG A:HIS116 4.2 31.0 1.0 ND1 A:HIS116 4.2 28.2 1.0 O A:HOH2053 4.3 37.8 1.0 HG2 B:GLU62 4.4 48.6 1.0 CG2 A:THR197 4.4 23.6 1.0 HD2 A:TYR233 4.4 51.5 1.0 HB3 A:OCS221 4.5 38.5 1.0 CB A:OCS221 4.6 32.1 1.0 HG3 B:GLU62 4.6 48.6 1.0 H A:HIS118 4.7 42.4 1.0 CA A:HIS118 4.7 41.7 1.0 HG2 A:ARG121 4.7 49.6 0.6 HD2 A:HIS196 4.8 23.7 1.0 HG23 A:THR197 4.8 28.3 1.0 HG3 A:ARG121 4.8 49.6 0.6 CG A:ASP120 4.8 34.8 0.5 HE2 A:HIS118 4.9 40.3 1.0 SG A:OCS221 5.0 33.6 1.0 OD2 A:ASP120 5.0 33.4 0.5 HD2 A:HIS118 5.0 38.0 1.0

Zinc binding site 2 out of 2 in the W228S-Investigation of the Impact From Residues W228 and Y233 in the Metallo-Beta-Lactamase Gim-1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of W228S-Investigation of the Impact From Residues W228 and Y233 in the Metallo-Beta-Lactamase Gim-1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1296 b:37.0 occ:1.00 NE2 B:HIS196 2.0 33.2 1.0 OE2 A:GLU62 2.0 39.4 1.0 ND1 B:HIS118 2.1 37.5 1.0 NE2 B:HIS116 2.2 28.8 1.0 CD A:GLU62 2.7 44.0 1.0 OE1 A:GLU62 2.8 38.2 1.0 CE1 B:HIS196 2.9 34.6 1.0 CD2 B:HIS116 3.0 30.1 1.0 HE1 B:HIS196 3.0 41.5 1.0 CD2 B:HIS196 3.0 33.3 1.0 CE1 B:HIS118 3.0 37.8 1.0 HB2 B:HIS118 3.1 52.3 1.0 HD2 B:HIS116 3.1 36.1 1.0 CG B:HIS118 3.1 38.6 1.0 HE1 B:HIS118 3.2 45.3 1.0 CE1 B:HIS116 3.2 30.4 1.0 HD2 B:HIS196 3.3 39.9 1.0 CB B:HIS118 3.5 43.6 1.0 HE1 B:HIS116 3.5 36.5 1.0 HB3 B:HIS118 3.6 52.3 1.0 HG21 B:THR197 3.8 42.3 1.0 HG22 B:THR197 3.9 42.3 1.0 ND1 B:HIS196 4.0 39.1 1.0 HB2 B:OCS221 4.0 45.0 1.0 CG B:HIS196 4.1 39.9 1.0 NE2 B:HIS118 4.2 35.8 1.0 CG A:GLU62 4.2 42.0 1.0 CD2 B:HIS118 4.2 36.0 1.0 CG B:HIS116 4.2 28.6 1.0 OD2 B:OCS221 4.3 46.8 1.0 ND1 B:HIS116 4.3 30.1 1.0 CG2 B:THR197 4.3 35.2 1.0 HD2 B:TYR233 4.4 53.4 1.0 HG2 A:GLU62 4.4 50.3 1.0 O A:HOH2019 4.5 49.6 1.0 HB3 B:OCS221 4.5 45.0 1.0 HG3 A:GLU62 4.6 50.3 1.0 CB B:OCS221 4.6 37.5 1.0 HG23 B:THR197 4.7 42.3 1.0 H B:HIS118 4.7 44.7 1.0 HD1 B:HIS196 4.8 46.9 1.0 HE2 B:HIS118 4.9 43.0 1.0 CA B:HIS118 4.9 44.6 1.0

S.Skagseth, T.J.Carlsen, G.E.K.Bjerga, J.Spencer, O.Samuelsen, H.S.Leiros. Role of Residues W228 and Y233 in the Structure and Activity of Metallo-Beta-Lactamase Gim-1. Antimicrob.Agents Chemother. V. 60 990 2015.
ISSN: ISSN 0066-4804
PubMed: 26643332
DOI: 10.1128/AAC.02017-15