Zinc in PDB 6v73: Crystal Structure of Metallo Beta Lactamase From Erythrobacter Litoralis with Beta Mercaptoethanol in the Active Site

The structure of Crystal Structure of Metallo Beta Lactamase From Erythrobacter Litoralis with Beta Mercaptoethanol in the Active Site, PDB code: 6v73 was solved by N.Maltseva, Y.Kim, S.Clancy, M.Endres, R.Mulligan, A.Joachimiak, Center Forstructural Genomics Of Infectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.65 / 2.40
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	121.139, 121.139, 90.551, 90.00, 90.00, 120.00
R / Rfree (%)	18 / 24.1

The structure of Crystal Structure of Metallo Beta Lactamase From Erythrobacter Litoralis with Beta Mercaptoethanol in the Active Site also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Zinc atom in the Crystal Structure of Metallo Beta Lactamase From Erythrobacter Litoralis with Beta Mercaptoethanol in the Active Site (pdb code 6v73). 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 Metallo Beta Lactamase From Erythrobacter Litoralis with Beta Mercaptoethanol in the Active Site, PDB code: 6v73:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Metallo Beta Lactamase From Erythrobacter Litoralis with Beta Mercaptoethanol in the Active Site


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 Metallo Beta Lactamase From Erythrobacter Litoralis with Beta Mercaptoethanol in the Active Site within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:51.6 occ:1.00 S2 A:BME304 2.1 68.2 1.0 NE2 A:HIS181 2.1 66.9 1.0 ND1 A:HIS114 2.1 50.1 1.0 NE2 A:HIS112 2.1 58.7 1.0 CD2 A:HIS181 3.0 56.2 1.0 CG A:HIS114 3.0 47.9 1.0 C2 A:BME304 3.1 67.8 1.0 CE1 A:HIS114 3.1 50.9 1.0 CD2 A:HIS112 3.1 57.9 1.0 CE1 A:HIS112 3.1 59.7 1.0 CE1 A:HIS181 3.1 63.2 1.0 CB A:HIS114 3.3 46.9 1.0 ZN A:ZN302 3.5 61.6 1.0 SG A:CYS200 3.8 56.3 1.0 C1 A:BME304 4.0 63.4 1.0 CB A:CYS200 4.1 62.3 1.0 OD2 A:ASP116 4.2 58.4 1.0 NE2 A:HIS114 4.2 47.9 1.0 CD2 A:HIS114 4.2 46.1 1.0 CG A:HIS181 4.2 56.0 1.0 ND1 A:HIS181 4.2 61.5 1.0 ND1 A:HIS112 4.2 56.5 1.0 CG A:HIS112 4.2 59.5 1.0 CG2 A:THR182 4.5 61.2 1.0 OD1 A:ASP116 4.6 60.0 1.0 CA A:HIS114 4.8 51.7 1.0 CG A:ASP116 4.8 56.0 1.0 O A:HOH422 4.8 50.2 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Metallo Beta Lactamase From Erythrobacter Litoralis with Beta Mercaptoethanol in the Active Site


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 Metallo Beta Lactamase From Erythrobacter Litoralis with Beta Mercaptoethanol in the Active Site within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:61.6 occ:1.00 S2 A:BME304 2.0 68.2 1.0 NE2 A:HIS242 2.1 62.6 1.0 SG A:CYS200 2.3 56.3 1.0 OD1 A:ASP116 2.5 60.0 1.0 CD2 A:HIS242 3.0 56.5 1.0 C2 A:BME304 3.1 67.8 1.0 CE1 A:HIS242 3.2 54.4 1.0 CB A:CYS200 3.3 62.3 1.0 O A:HOH422 3.4 50.2 1.0 CG A:ASP116 3.5 56.0 1.0 ZN A:ZN301 3.5 51.6 1.0 OD2 A:ASP116 3.9 58.4 1.0 NE2 A:HIS181 4.2 66.9 1.0 CG A:HIS242 4.2 58.9 1.0 C1 A:BME304 4.2 63.4 1.0 ND1 A:HIS242 4.2 59.4 1.0 CB A:SER241 4.4 52.6 1.0 CE1 A:HIS181 4.4 63.2 1.0 CA A:CYS200 4.5 55.5 1.0 O1 A:BME304 4.6 72.4 1.0 NE2 A:HIS112 4.7 58.7 1.0 OG A:SER241 4.8 57.8 1.0 CE1 A:HIS112 4.8 59.7 1.0 CB A:ASP116 4.8 52.9 1.0

N.Maltseva, Y.Kim, S.Clancy, M.Endres, R.Mulligan, A.Joachimiak, Center For Structural Genomics Of Infectious Diseases(Csgid). Crystal Structure of Metallo Beta Lactamase From Erythrobacter Litoralis with Beta Mercaptoethanol in the Active Site To Be Published.