Zinc in PDB 2m5c: Solution Structure of the Bacillus Cereus Metallo-Beta-Lactamase Bcii

All present enzymatic activity of Solution Structure of the Bacillus Cereus Metallo-Beta-Lactamase Bcii:
3.5.2.6;

The binding sites of Zinc atom in the Solution Structure of the Bacillus Cereus Metallo-Beta-Lactamase Bcii (pdb code 2m5c). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Solution Structure of the Bacillus Cereus Metallo-Beta-Lactamase Bcii, PDB code: 2m5c:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Solution Structure of the Bacillus Cereus Metallo-Beta-Lactamase Bcii


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Solution Structure of the Bacillus Cereus Metallo-Beta-Lactamase Bcii within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:42.5 occ:1.00 HE2 A:HIS149 1.7 0.0 1.0 HE2 A:HIS86 2.0 0.0 1.0 NE2 A:HIS149 2.3 53.2 1.0 NE2 A:HIS86 2.4 10.3 1.0 ND1 A:HIS88 2.4 14.3 1.0 HD2 A:ASP90 2.5 0.0 1.0 HD2 A:HIS149 2.5 31.3 1.0 CD2 A:HIS149 2.6 71.3 1.0 CG A:HIS88 2.8 24.3 1.0 HB2 A:HIS88 2.8 0.0 1.0 HB2 A:CYS168 3.0 0.0 1.0 CE1 A:HIS86 3.1 71.1 1.0 CB A:HIS88 3.1 74.3 1.0 HB3 A:HIS88 3.1 72.3 1.0 CE1 A:HIS88 3.2 62.3 1.0 OD1 A:ASP90 3.2 20.6 1.0 CD2 A:HIS86 3.3 23.2 1.0 HE1 A:HIS86 3.3 1.2 1.0 OD2 A:ASP90 3.4 23.0 1.0 CE1 A:HIS149 3.4 61.0 1.0 HB3 A:CYS168 3.4 0.2 1.0 SG A:CYS168 3.5 44.0 1.0 CB A:CYS168 3.5 53.4 1.0 HD2 A:HIS86 3.6 51.5 1.0 CD2 A:HIS88 3.7 41.3 1.0 CG A:ASP90 3.7 23.0 1.0 HE1 A:HIS88 3.7 4.2 1.0 HD3 A:ARG91 3.8 35.1 1.0 CG A:HIS149 3.8 22.4 1.0 ZN A:ZN302 3.9 12.2 1.0 NE2 A:HIS88 3.9 63.5 1.0 HH11 A:ARG91 3.9 74.2 1.0 HE1 A:HIS149 4.0 42.5 1.0 ND1 A:HIS86 4.0 33.2 1.0 CG A:HIS86 4.2 64.3 1.0 ND1 A:HIS149 4.2 33.2 1.0 HG21 A:THR150 4.3 32.0 1.0 NH1 A:ARG91 4.4 52.4 1.0 HD2 A:HIS88 4.5 52.3 1.0 HG23 A:THR150 4.5 61.1 1.0 CA A:HIS88 4.6 73.0 1.0 HH12 A:ARG91 4.7 12.5 1.0 HE2 A:HIS88 4.7 4.5 1.0 CG2 A:THR150 4.8 13.4 1.0 HG22 A:THR150 4.8 42.3 1.0 CD A:ARG91 4.8 73.1 1.0 HD1 A:HIS86 4.8 54.2 1.0 H A:ASP90 4.9 5.2 1.0 HB3 A:HIS149 4.9 4.4 1.0 H A:CYS168 4.9 32.4 1.0 CA A:CYS168 5.0 43.3 1.0

Zinc binding site 2 out of 2 in the Solution Structure of the Bacillus Cereus Metallo-Beta-Lactamase Bcii


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Solution Structure of the Bacillus Cereus Metallo-Beta-Lactamase Bcii within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:12.2 occ:1.00 HE2 A:HIS210 1.7 0.0 1.0 SG A:CYS168 2.2 44.0 1.0 OD2 A:ASP90 2.4 23.0 1.0 HD2 A:ASP90 2.4 0.0 1.0 NE2 A:HIS210 2.5 11.5 1.0 CG A:ASP90 3.0 23.0 1.0 CE1 A:HIS210 3.2 63.4 1.0 HE1 A:HIS210 3.3 74.4 1.0 CD2 A:HIS210 3.6 65.2 1.0 OD1 A:ASP90 3.6 20.6 1.0 HH12 A:ARG91 3.7 12.5 1.0 HB3 A:ASP90 3.7 32.2 1.0 HH2 A:TRP59 3.7 55.1 1.0 HH11 A:ARG91 3.8 74.2 1.0 CB A:ASP90 3.8 1.2 1.0 CB A:CYS168 3.8 53.4 1.0 ZN A:ZN301 3.9 42.5 1.0 HD2 A:HIS210 3.9 70.2 1.0 HB2 A:ASP90 3.9 0.0 1.0 HB2 A:CYS168 4.0 0.0 1.0 NH1 A:ARG91 4.1 52.4 1.0 HE2 A:HIS149 4.2 0.0 1.0 ND1 A:HIS210 4.3 1.0 1.0 HA3 A:GLY209 4.4 31.5 1.0 HB3 A:CYS168 4.5 0.2 1.0 CH2 A:TRP59 4.5 24.2 1.0 HE1 A:HIS149 4.5 42.5 1.0 HA A:CYS168 4.5 71.4 1.0 CG A:HIS210 4.5 23.2 1.0 HE2 A:HIS86 4.6 0.0 1.0 O A:GLY209 4.6 64.5 1.0 NE2 A:HIS149 4.6 53.2 1.0 CA A:CYS168 4.8 43.3 1.0 CE1 A:HIS149 4.8 61.0 1.0 CD2 A:HIS88 4.9 41.3 1.0 HZ3 A:TRP59 5.0 45.0 1.0 NE2 A:HIS88 5.0 63.5 1.0

A.I.Karsisiotis, C.F.Damblon, G.C.K.Roberts. Solution Structures of the Bacillus Cereus Metallo-Beta-Lactamase Bcii and Its Complex with the Broad Spectrum Inhibitor R-Thiomandelic Acid Biochem.J. 2013.
ISSN: ESSN 1470-8728
PubMed: 24059435
DOI: 10.1042/BJ20131003