Zinc in PDB 9gx9: Crystal Structure of Cjo-1, A Membrane-Bound B1 Metallo-Beta-Lactamase From Chryseobacterium Joostei

All present enzymatic activity of Crystal Structure of Cjo-1, A Membrane-Bound B1 Metallo-Beta-Lactamase From Chryseobacterium Joostei:
3.5.2.6;

The structure of Crystal Structure of Cjo-1, A Membrane-Bound B1 Metallo-Beta-Lactamase From Chryseobacterium Joostei, PDB code: 9gx9 was solved by P.Hinchliffe, J.Spencer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	67.50 / 1.34
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	47.517, 68.156, 135.004, 90, 90, 90
R / Rfree (%)	14.2 / 17.2

The binding sites of Zinc atom in the Crystal Structure of Cjo-1, A Membrane-Bound B1 Metallo-Beta-Lactamase From Chryseobacterium Joostei (pdb code 9gx9). 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 Cjo-1, A Membrane-Bound B1 Metallo-Beta-Lactamase From Chryseobacterium Joostei, PDB code: 9gx9:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Cjo-1, A Membrane-Bound B1 Metallo-Beta-Lactamase From Chryseobacterium Joostei


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 Cjo-1, A Membrane-Bound B1 Metallo-Beta-Lactamase From Chryseobacterium Joostei within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:19.2 occ:1.00 O A:HOH427 1.9 20.3 1.0 NE2 A:HIS93 2.1 15.2 1.0 NE2 A:HIS156 2.1 14.8 1.0 ND1 A:HIS95 2.2 15.4 1.0 HB2 A:HIS95 3.0 17.6 1.0 CD2 A:HIS156 3.0 15.8 1.0 CD2 A:HIS93 3.0 13.7 1.0 CE1 A:HIS95 3.1 16.6 1.0 CG A:HIS95 3.1 14.7 1.0 CE1 A:HIS156 3.1 15.9 1.0 CE1 A:HIS93 3.1 14.5 1.0 HD2 A:HIS93 3.2 16.5 1.0 HD2 A:HIS156 3.2 18.9 1.0 HE1 A:HIS95 3.3 19.9 1.0 HE1 A:HIS156 3.4 19.1 1.0 HE1 A:HIS93 3.4 17.4 1.0 ZN A:ZN303 3.4 21.6 0.7 CB A:HIS95 3.5 14.6 1.0 HB3 A:HIS95 3.6 17.6 1.0 HB2 A:CSO175 3.7 22.9 0.9 SG A:CSO175 3.8 37.5 0.1 HB2 A:CSO175 3.8 38.0 0.1 OD1 A:ASP97 3.8 22.4 1.0 HB3 A:CSO175 3.9 22.9 0.9 HB3 A:CSO175 3.9 38.0 0.1 O A:HOH521 3.9 20.9 1.0 CB A:CSO175 4.0 31.6 0.1 HG23 A:THR157 4.1 17.7 1.0 CB A:CSO175 4.1 19.1 0.9 SG A:CSO175 4.2 17.5 0.9 CG A:HIS156 4.2 14.6 1.0 NE2 A:HIS95 4.2 17.4 1.0 CG A:HIS93 4.2 14.4 1.0 ND1 A:HIS93 4.2 15.1 1.0 ND1 A:HIS156 4.2 14.9 1.0 CD2 A:HIS95 4.3 16.5 1.0 OD2 A:ASP97 4.3 20.1 1.0 HG21 A:THR157 4.3 17.7 1.0 CG A:ASP97 4.5 19.3 1.0 CG2 A:THR157 4.7 14.7 1.0 H A:HIS95 4.7 16.0 1.0 HD2 A:TYR186 4.7 26.5 1.0 CA A:HIS95 4.9 13.8 1.0 HE2 A:HIS95 5.0 20.9 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Cjo-1, A Membrane-Bound B1 Metallo-Beta-Lactamase From Chryseobacterium Joostei


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 Cjo-1, A Membrane-Bound B1 Metallo-Beta-Lactamase From Chryseobacterium Joostei within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn303 b:21.6 occ:0.71 SG A:CSO175 1.9 37.5 0.1 O A:HOH427 2.0 20.3 1.0 SG A:CSO175 2.2 17.5 0.9 NE2 A:HIS216 2.2 19.6 1.0 O A:HOH521 2.3 20.9 1.0 OD2 A:ASP97 2.3 20.1 1.0 OD A:CSO175 2.3 41.0 0.1 HB3 A:CSO175 3.0 22.9 0.9 CD2 A:HIS216 3.0 19.3 1.0 HD2 A:HIS216 3.1 23.2 1.0 CB A:CSO175 3.2 19.1 0.9 CG A:ASP97 3.3 19.3 1.0 CE1 A:HIS216 3.3 20.8 1.0 ZN A:ZN302 3.4 19.2 1.0 CB A:CSO175 3.4 31.6 0.1 HB2 A:CSO175 3.5 38.0 0.1 HE1 A:HIS93 3.6 17.4 1.0 HE1 A:HIS216 3.6 24.9 1.0 OD1 A:ASP97 3.6 22.4 1.0 HB2 A:CSO175 3.7 22.9 0.9 HB3 A:CSO175 3.9 38.0 0.1 NE2 A:HIS156 4.1 14.8 1.0 O A:HOH510 4.1 16.8 1.0 CE1 A:HIS93 4.2 14.5 1.0 NE2 A:HIS93 4.2 15.2 1.0 HA A:CSO175 4.2 27.6 0.1 CG A:HIS216 4.2 17.7 1.0 HA A:CSO175 4.3 18.0 0.9 ND1 A:HIS216 4.3 19.4 1.0 HE1 A:HIS156 4.3 19.1 1.0 O A:HOH454 4.4 17.9 1.0 HA3 A:GLY215 4.4 15.8 1.0 CE1 A:HIS156 4.4 15.9 1.0 CA A:CSO175 4.4 15.0 0.9 CA A:CSO175 4.4 23.0 0.1 CB A:ASP97 4.6 16.3 1.0 HB2 A:ASP97 4.6 19.6 1.0 O A:HOH563 4.8 15.6 1.0 CD2 A:HIS156 4.9 15.8 1.0 HB3 A:ASP97 5.0 19.6 1.0

M.C.Carnevale, A.R.Palacios, P.Hinchliffe, J.Delmonti, S.I.Drusin, D.M.Moreno, R.A.Bonomo, J.Spencer, A.J.Vila. Active Site Loops of Membrane-Anchored Metallo-Beta-Lactamases From Environmental Bacteria Determine Cephalosporinase Activity. Antimicrob.Agents Chemother. 91824 2025.
ISSN: ESSN 1098-6596
PubMed: 40548716
DOI: 10.1128/AAC.01918-24