Zinc in PDB 1bc2: Zn-Dependent Metallo-Beta-Lactamase From Bacillus Cereus

All present enzymatic activity of Zn-Dependent Metallo-Beta-Lactamase From Bacillus Cereus:
3.5.2.6;

The structure of Zn-Dependent Metallo-Beta-Lactamase From Bacillus Cereus, PDB code: 1bc2 was solved by S.M.Fabiane, B.J.Sutton, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 1.90
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	67.630, 67.630, 178.380, 90.00, 90.00, 120.00
R / Rfree (%)	20.8 / 27.9

The binding sites of Zinc atom in the Zn-Dependent Metallo-Beta-Lactamase From Bacillus Cereus (pdb code 1bc2). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Zn-Dependent Metallo-Beta-Lactamase From Bacillus Cereus, PDB code: 1bc2:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Zn-Dependent Metallo-Beta-Lactamase From Bacillus Cereus


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Zn-Dependent Metallo-Beta-Lactamase From Bacillus Cereus within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn228 b:31.1 occ:1.00 O A:HOH400 1.9 40.7 1.0 ND1 A:HIS88 2.0 27.0 1.0 NE2 A:HIS149 2.0 26.9 1.0 NE2 A:HIS86 2.3 19.4 1.0 CG A:HIS88 2.9 30.7 1.0 CE1 A:HIS88 2.9 28.5 1.0 CD2 A:HIS149 3.0 23.7 1.0 CE1 A:HIS149 3.0 27.2 1.0 CD2 A:HIS86 3.1 19.5 1.0 CB A:HIS88 3.3 28.7 1.0 CE1 A:HIS86 3.3 21.1 1.0 ZN A:ZN229 3.8 53.0 1.0 NE2 A:HIS88 4.0 27.9 1.0 CD2 A:HIS88 4.0 28.9 1.0 ND1 A:HIS149 4.1 27.8 1.0 CG A:HIS149 4.1 27.7 1.0 OD1 A:ASP90 4.2 32.6 1.0 CG A:HIS86 4.3 19.8 1.0 SG A:CYS168 4.3 36.0 1.0 ND1 A:HIS86 4.3 22.2 1.0 CG2 A:THR150 4.4 20.2 1.0 CB A:CYS168 4.4 30.7 1.0 O A:HOH313 4.4 26.1 1.0 O A:HOH412 4.5 53.7 1.0 O A:HOH415 4.7 34.8 1.0 O A:HOH237 4.7 22.3 1.0 CA A:HIS88 4.7 27.4 1.0

Zinc binding site 2 out of 4 in the Zn-Dependent Metallo-Beta-Lactamase From Bacillus Cereus


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Zn-Dependent Metallo-Beta-Lactamase From Bacillus Cereus within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn229 b:53.0 occ:1.00 SG A:CYS168 1.9 36.0 1.0 O A:HOH400 2.5 40.7 1.0 O A:HOH313 2.6 26.1 1.0 NE2 A:HIS210 2.6 38.7 1.0 OD2 A:ASP90 2.7 34.5 1.0 CB A:CYS168 3.2 30.7 1.0 CD2 A:HIS210 3.3 37.0 1.0 CG A:ASP90 3.7 33.2 1.0 CE1 A:HIS210 3.7 35.6 1.0 ZN A:ZN228 3.8 31.1 1.0 OD1 A:ASP90 3.9 32.6 1.0 NH2 A:ARG91 3.9 28.0 1.0 NE A:ARG91 4.2 25.2 1.0 O A:HOH383 4.2 31.8 1.0 CE1 A:HIS86 4.3 21.1 1.0 NE2 A:HIS149 4.3 26.9 1.0 CA A:CYS168 4.3 27.1 1.0 NE2 A:HIS86 4.4 19.4 1.0 CZ A:ARG91 4.5 25.4 1.0 CG A:HIS210 4.5 33.8 1.0 ND1 A:HIS210 4.7 34.6 1.0 O A:HOH415 4.7 34.8 1.0 CE1 A:HIS149 4.7 27.2 1.0 O A:HOH319 4.9 40.4 1.0 N A:CYS168 4.9 27.1 1.0 CD2 A:HIS149 4.9 23.7 1.0 CB A:ASP90 5.0 28.8 1.0

Zinc binding site 3 out of 4 in the Zn-Dependent Metallo-Beta-Lactamase From Bacillus Cereus


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Zn-Dependent Metallo-Beta-Lactamase From Bacillus Cereus within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn228 b:31.6 occ:1.00 O B:HOH302 1.9 32.1 1.0 NE2 B:HIS149 2.1 27.1 1.0 ND1 B:HIS88 2.2 38.9 1.0 NE2 B:HIS86 2.2 26.3 1.0 CD2 B:HIS149 3.0 25.9 1.0 CG B:HIS88 3.1 36.1 1.0 CE1 B:HIS88 3.1 39.2 1.0 CE1 B:HIS86 3.1 25.0 1.0 CE1 B:HIS149 3.2 27.3 1.0 CD2 B:HIS86 3.2 23.8 1.0 CB B:HIS88 3.4 30.8 1.0 CG B:HIS149 4.2 24.7 1.0 NE2 B:HIS88 4.2 39.1 1.0 CD2 B:HIS88 4.2 38.6 1.0 ND1 B:HIS149 4.2 24.6 1.0 OD1 B:ASP90 4.3 33.6 1.0 ND1 B:HIS86 4.3 23.3 1.0 CG B:HIS86 4.3 25.8 1.0 ZN B:ZN229 4.4 61.5 1.0 SG B:CYS168 4.4 29.4 1.0 CG2 B:THR150 4.5 23.6 1.0 CB B:CYS168 4.5 28.7 1.0 CA B:HIS88 4.9 29.0 1.0 O B:HOH392 4.9 41.5 1.0 O B:HOH386 4.9 56.5 1.0 O B:HOH292 4.9 26.5 1.0 O B:HOH237 4.9 21.6 1.0 OD2 B:ASP90 4.9 35.9 1.0

Zinc binding site 4 out of 4 in the Zn-Dependent Metallo-Beta-Lactamase From Bacillus Cereus


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Zn-Dependent Metallo-Beta-Lactamase From Bacillus Cereus within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn229 b:61.5 occ:1.00 SG B:CYS168 2.0 29.4 1.0 NE2 B:HIS210 2.5 36.8 1.0 O B:HOH292 2.7 26.5 1.0 OD2 B:ASP90 2.9 35.9 1.0 O B:HOH302 3.1 32.1 1.0 CB B:CYS168 3.2 28.7 1.0 CE1 B:HIS210 3.3 30.4 1.0 CD2 B:HIS210 3.4 35.7 1.0 CG B:ASP90 4.0 31.6 1.0 NH2 B:ARG91 4.1 32.8 1.0 CA B:CYS168 4.2 26.1 1.0 O B:HOH392 4.3 41.5 1.0 ND1 B:HIS210 4.4 35.5 1.0 ZN B:ZN228 4.4 31.6 1.0 OD1 B:ASP90 4.4 33.6 1.0 CG B:HIS210 4.4 32.0 1.0 NE2 B:HIS149 4.5 27.1 1.0 NE B:ARG91 4.6 29.5 1.0 CZ B:ARG91 4.7 28.2 1.0 CE1 B:HIS86 4.8 25.0 1.0 CE1 B:HIS149 4.8 27.3 1.0 N B:CYS168 4.9 25.8 1.0

S.M.Fabiane, M.K.Sohi, T.Wan, D.J.Payne, J.H.Bateson, T.Mitchell, B.J.Sutton. Crystal Structure of the Zinc-Dependent Beta-Lactamase From Bacillus Cereus at 1.9 A Resolution: Binuclear Active Site with Features of A Mononuclear Enzyme. Biochemistry V. 37 12404 1998.
ISSN: ISSN 0006-2960
PubMed: 9730812
DOI: 10.1021/BI980506I