Zinc in PDB 5acr: W228Y-Investigation of the Impact From Residues W228 and Y233 in the Metallo-Beta-Lactamase Gim-1

The structure of W228Y-Investigation of the Impact From Residues W228 and Y233 in the Metallo-Beta-Lactamase Gim-1, PDB code: 5acr 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)	24.747 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	38.532, 129.732, 40.396, 90.00, 96.50, 90.00
R / Rfree (%)	20.17 / 24.42

The structure of W228Y-Investigation of the Impact From Residues W228 and Y233 in the Metallo-Beta-Lactamase Gim-1 also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Zinc atom in the W228Y-Investigation of the Impact From Residues W228 and Y233 in the Metallo-Beta-Lactamase Gim-1 (pdb code 5acr). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the W228Y-Investigation of the Impact From Residues W228 and Y233 in the Metallo-Beta-Lactamase Gim-1, PDB code: 5acr:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the W228Y-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 W228Y-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:Zn1296 b:24.1 occ:1.00 ND1 A:HIS118 1.9 23.7 1.0 NE2 A:HIS196 2.1 23.4 1.0 O A:HOH2070 2.1 23.2 1.0 NE2 A:HIS116 2.3 21.7 1.0 O A:HOH2073 2.5 19.8 1.0 CE1 A:HIS118 2.9 26.7 1.0 CG A:HIS118 2.9 23.7 1.0 CE1 A:HIS196 2.9 26.8 1.0 CD2 A:HIS196 3.2 23.6 1.0 CE1 A:HIS116 3.2 21.1 1.0 CB A:HIS118 3.3 23.1 1.0 CD2 A:HIS116 3.3 22.6 1.0 OD2 A:OCS221 3.7 20.9 1.0 NE2 A:HIS118 4.0 27.8 1.0 CD2 A:HIS118 4.0 24.4 1.0 OD1 A:ASP120 4.1 24.6 1.0 ND1 A:HIS196 4.1 21.9 1.0 CG A:HIS196 4.2 23.9 1.0 O A:HOH2078 4.2 37.1 1.0 ND1 A:HIS116 4.3 17.0 1.0 CG A:HIS116 4.4 20.7 1.0 O A:HOH2159 4.5 35.4 1.0 SG A:OCS221 4.5 23.4 1.0 CB A:OCS221 4.5 21.5 1.0 OD1 A:OCS221 4.6 20.1 0.9 CG2 A:THR197 4.7 22.9 1.0 CA A:HIS118 4.7 23.6 1.0 CD1 B:ILE61 4.8 52.9 0.0 O A:HOH2143 4.9 38.1 1.0 OD2 A:ASP120 4.9 33.3 1.0 CG A:ASP120 5.0 28.8 1.0

Zinc binding site 2 out of 2 in the W228Y-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 W228Y-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:40.3 occ:1.00 ND1 B:HIS118 1.9 47.4 1.0 NE2 B:HIS196 1.9 50.8 1.0 O B:HOH2029 2.2 35.4 1.0 CE1 B:HIS116 2.3 37.7 1.0 CE1 B:HIS118 2.5 49.8 1.0 CD2 B:HIS196 2.7 43.0 1.0 CG B:HIS118 2.8 45.3 1.0 CE1 B:HIS196 3.1 45.9 1.0 ND1 B:HIS116 3.1 47.7 1.0 CB B:HIS118 3.4 42.3 1.0 NE2 B:HIS116 3.4 44.6 1.0 NE2 B:HIS118 3.4 48.8 1.0 CD2 B:HIS118 3.6 46.8 1.0 OD2 B:OCS221 3.8 39.2 1.0 CG B:HIS196 3.9 50.6 1.0 OD1 B:ASP120 3.9 43.6 1.0 ND1 B:HIS196 4.0 52.6 1.0 CB B:OCS221 4.2 50.4 1.0 OD3 B:OCS221 4.2 46.1 1.0 SG B:OCS221 4.3 45.0 1.0 CG2 B:THR197 4.3 51.1 1.0 CG B:HIS116 4.4 43.2 1.0 CD2 B:HIS116 4.5 42.5 1.0 N A:GLY63 4.6 53.0 1.0 OD2 B:ASP120 4.8 44.7 1.0 CG B:ASP120 4.8 43.1 1.0 CA B:HIS118 4.8 41.7 1.0 O A:HOH2027 4.9 43.5 1.0 CA A:GLY63 5.0 53.7 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