Zinc in PDB 1x8h: The Mono-Zinc Carbapenemase Cpha (N220G Mutant) Shows A Zn(II)- NH2 Arg Coordination

All present enzymatic activity of The Mono-Zinc Carbapenemase Cpha (N220G Mutant) Shows A Zn(II)- NH2 Arg Coordination:
3.5.2.6;

The structure of The Mono-Zinc Carbapenemase Cpha (N220G Mutant) Shows A Zn(II)- NH2 Arg Coordination, PDB code: 1x8h was solved by G.Garau, O.Dideberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.60
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	42.683, 101.286, 117.820, 90.00, 90.00, 90.00
R / Rfree (%)	15.3 / 18

The binding sites of Zinc atom in the The Mono-Zinc Carbapenemase Cpha (N220G Mutant) Shows A Zn(II)- NH2 Arg Coordination (pdb code 1x8h). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the The Mono-Zinc Carbapenemase Cpha (N220G Mutant) Shows A Zn(II)- NH2 Arg Coordination, PDB code: 1x8h:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the The Mono-Zinc Carbapenemase Cpha (N220G Mutant) Shows A Zn(II)- NH2 Arg Coordination


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Mono-Zinc Carbapenemase Cpha (N220G Mutant) Shows A Zn(II)- NH2 Arg Coordination within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:9.5 occ:0.75 ZN A:ZN401 0.0 9.5 0.8 ZN A:ZN401 1.6 11.5 0.2 OD2 A:ASP120 2.0 13.2 1.0 O1 A:CO32 2.0 22.0 1.0 NE2 A:HIS263 2.1 10.9 1.0 SG A:CYS221 2.3 10.5 1.0 C A:CO32 2.8 23.5 1.0 O2 A:CO32 2.9 23.3 1.0 CE1 A:HIS263 3.0 10.3 1.0 CG A:ASP120 3.0 11.8 1.0 CD2 A:HIS263 3.2 10.3 1.0 OD1 A:ASP120 3.2 15.4 1.0 CB A:CYS221 3.3 10.7 1.0 NH2 A:ARG121 3.8 9.8 0.8 NH2 A:ARG121 3.9 9.6 0.2 O A:HOH403 3.9 30.3 1.0 O3 A:CO32 4.0 26.8 1.0 CA A:CYS221 4.1 10.4 1.0 ND1 A:HIS263 4.1 10.0 1.0 O A:HOH445 4.2 28.7 1.0 CG A:HIS263 4.2 9.0 1.0 CB A:ASP120 4.3 8.8 1.0 NE A:ARG121 4.4 9.0 0.2 NE A:ARG121 4.4 8.9 0.8 CZ A:ARG121 4.5 9.0 0.2 CZ A:ARG121 4.5 8.3 0.8 CE1 A:HIS196 4.6 11.2 1.0 NE2 A:HIS196 4.6 12.4 1.0 O A:HOH572 4.8 25.5 1.0 N A:CYS221 4.8 11.0 1.0 O A:HOH406 4.9 28.4 1.0

Zinc binding site 2 out of 2 in the The Mono-Zinc Carbapenemase Cpha (N220G Mutant) Shows A Zn(II)- NH2 Arg Coordination


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Mono-Zinc Carbapenemase Cpha (N220G Mutant) Shows A Zn(II)- NH2 Arg Coordination within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:11.5 occ:0.25 ZN A:ZN401 0.0 11.5 0.2 ZN A:ZN401 1.6 9.5 0.8 SG A:CYS221 2.1 10.5 1.0 NE2 A:HIS263 2.1 10.9 1.0 OD2 A:ASP120 2.2 13.2 1.0 NH2 A:ARG121 2.3 9.8 0.8 NH2 A:ARG121 2.3 9.6 0.2 CZ A:ARG121 3.0 9.0 0.2 CZ A:ARG121 3.0 8.3 0.8 CE1 A:HIS263 3.0 10.3 1.0 CD2 A:HIS263 3.0 10.3 1.0 NE A:ARG121 3.1 9.0 0.2 NE A:ARG121 3.1 8.9 0.8 CG A:ASP120 3.1 11.8 1.0 CB A:CYS221 3.3 10.7 1.0 O1 A:CO32 3.5 22.0 1.0 OD1 A:ASP120 3.5 15.4 1.0 CA A:CYS221 3.6 10.4 1.0 N A:CYS221 3.9 11.0 1.0 ND1 A:HIS263 4.0 10.0 1.0 O2 A:CO32 4.0 23.3 1.0 CG A:HIS263 4.1 9.0 1.0 NH1 A:ARG121 4.1 9.9 0.2 NH1 A:ARG121 4.1 10.6 0.8 C A:CO32 4.2 23.5 1.0 O A:GLY262 4.2 8.1 1.0 CB A:ASP120 4.3 8.8 1.0 CD A:ARG121 4.4 8.5 0.2 CD A:ARG121 4.4 8.3 0.8 C A:GLY220 4.6 11.2 1.0 CG A:ARG121 4.7 7.8 0.8 CG A:ARG121 4.7 8.0 0.2 C A:GLY262 4.8 7.8 1.0 CB A:GLU69 4.9 7.0 1.0 C A:CYS221 5.0 9.8 1.0

G.Garau, C.Bebrone, C.Anne, M.Galleni, J.M.Frere, O.Dideberg. A Metallo-Beta-Lactamase Enzyme in Action: Crystal Structures of the Monozinc Carbapenemase Cpha and Its Complex with Biapenem J.Mol.Biol. V. 345 785 2005.
ISSN: ISSN 0022-2836
PubMed: 15588826
DOI: 10.1016/J.JMB.2004.10.070