Zinc in PDB 1k07: Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii

All present enzymatic activity of Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii:
3.5.2.6;

The structure of Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii, PDB code: 1k07 was solved by I.Garcia-Saez, P.S.Mercuri, R.Kahn, C.Papamicael, J.M.Frere, M.Galleni, O.Dideberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 1.65
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	44.860, 76.850, 78.890, 90.00, 102.08, 90.00
R / Rfree (%)	17.4 / 19.8

The binding sites of Zinc atom in the Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii (pdb code 1k07). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii, PDB code: 1k07:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1 b:8.1 occ:1.00 NE2 A:HIS196 2.1 5.3 1.0 ND1 A:HIS118 2.1 7.0 1.0 NE2 A:HIS116 2.1 5.6 1.0 O2 A:GOL1502 2.1 22.2 0.5 O1 A:GOL1502 2.6 20.2 0.5 C1 A:GOL1502 2.6 21.0 0.5 O1 A:GOL1502 2.9 23.8 0.5 CD2 A:HIS196 3.0 5.4 1.0 CE1 A:HIS118 3.0 6.7 1.0 CD2 A:HIS116 3.0 5.6 1.0 C2 A:GOL1502 3.0 23.1 0.5 CE1 A:HIS116 3.1 5.5 1.0 CE1 A:HIS196 3.1 6.0 1.0 CG A:HIS118 3.1 6.7 1.0 O A:HOH1588 3.3 4.1 0.5 CB A:HIS118 3.5 6.7 1.0 C1 A:GOL1502 3.5 23.1 0.5 ZN A:ZN2 3.7 10.7 1.0 C2 A:GOL1502 4.0 20.6 0.5 ND1 A:HIS116 4.1 5.0 1.0 CG A:HIS116 4.1 5.6 1.0 NE2 A:HIS118 4.1 7.2 1.0 CG A:HIS196 4.2 5.6 1.0 OD2 A:ASP120 4.2 7.8 1.0 ND1 A:HIS196 4.2 5.6 1.0 CD2 A:HIS118 4.2 7.0 1.0 CD2 A:HIS121 4.3 6.6 1.0 C3 A:GOL1502 4.4 23.2 0.5 NE2 A:HIS121 4.4 6.0 1.0 O A:HOH1588 4.4 6.2 0.5 ND2 A:ASN225 4.5 8.7 1.0 O3 A:GOL1502 4.6 20.8 0.5 O2 A:GOL1502 4.7 21.0 0.5 C3 A:GOL1502 4.7 21.3 0.5 OG A:SER221 4.7 8.5 0.3 OD1 A:ASP120 4.8 7.2 1.0 O3 A:GOL1502 4.9 23.7 0.5 CG2 A:THR197 4.9 6.5 1.0 CA A:HIS118 5.0 6.6 1.0 CG A:ASP120 5.0 7.3 1.0

Zinc binding site 2 out of 4 in the Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2 b:10.7 occ:1.00 NE2 A:HIS263 2.0 6.4 1.0 O2 A:GOL1502 2.1 22.2 0.5 OD1 A:ASP120 2.1 7.2 1.0 NE2 A:HIS121 2.2 6.0 1.0 O A:HOH1588 2.3 4.1 0.5 O3 A:GOL1502 2.4 23.7 0.5 O3 A:GOL1502 2.5 20.8 0.5 C3 A:GOL1502 3.0 23.2 0.5 CE1 A:HIS263 3.0 7.6 1.0 C2 A:GOL1502 3.0 23.1 0.5 CG A:ASP120 3.0 7.3 1.0 C3 A:GOL1502 3.0 21.3 0.5 CD2 A:HIS263 3.1 7.5 1.0 CE1 A:HIS121 3.1 6.1 1.0 CD2 A:HIS121 3.2 6.6 1.0 OD2 A:ASP120 3.3 7.8 1.0 C1 A:GOL1502 3.3 21.0 0.5 ZN A:ZN1 3.7 8.1 1.0 C2 A:GOL1502 3.8 20.6 0.5 NE2 A:HIS116 4.0 5.6 1.0 CE1 A:HIS116 4.1 5.5 1.0 ND1 A:HIS263 4.1 7.1 1.0 O A:HOH1588 4.1 6.2 0.5 C1 A:GOL1502 4.1 23.1 0.5 ND1 A:HIS121 4.2 6.2 1.0 CG A:HIS263 4.2 7.2 1.0 CG A:HIS121 4.2 6.3 1.0 CB A:ASP120 4.4 7.4 1.0 O1 A:GOL1502 4.6 20.2 0.5 O2 A:GOL1502 4.7 21.0 0.5 O1 A:GOL1502 4.8 23.8 0.5 OG A:SER262 5.0 6.5 1.0 NE2 A:HIS196 5.0 5.3 1.0

Zinc binding site 3 out of 4 in the Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn3 b:8.2 occ:1.00 NE2 B:HIS196 2.0 5.4 1.0 NE2 B:HIS116 2.1 5.9 1.0 ND1 B:HIS118 2.1 6.8 1.0 O2 B:GOL1503 2.2 18.9 0.5 O3 B:GOL1503 2.2 19.3 0.5 C1 B:GOL1503 2.6 20.2 0.5 O1 B:GOL1503 2.7 19.9 0.5 CD2 B:HIS196 3.0 5.2 1.0 CE1 B:HIS116 3.0 5.4 1.0 CE1 B:HIS118 3.0 6.8 1.0 CD2 B:HIS116 3.0 5.3 1.0 CE1 B:HIS196 3.1 6.0 1.0 CG B:HIS118 3.1 6.5 1.0 C2 B:GOL1503 3.2 19.4 0.5 C3 B:GOL1503 3.2 19.6 0.5 O B:HOH1565 3.3 4.3 0.5 CB B:HIS118 3.5 6.1 1.0 ZN B:ZN4 3.7 10.9 1.0 C2 B:GOL1503 4.0 19.7 0.5 ND1 B:HIS116 4.1 6.2 1.0 CG B:HIS196 4.1 5.0 1.0 CG B:HIS116 4.1 6.0 1.0 ND1 B:HIS196 4.2 6.0 1.0 NE2 B:HIS118 4.2 7.7 1.0 C1 B:GOL1503 4.2 19.8 0.5 OD2 B:ASP120 4.2 8.0 1.0 CD2 B:HIS118 4.2 7.1 1.0 CD2 B:HIS121 4.3 6.7 1.0 NE2 B:HIS121 4.4 5.9 1.0 O3 B:GOL1503 4.5 19.9 0.5 O B:HOH1565 4.6 6.5 0.5 ND2 B:ASN225 4.6 9.2 1.0 C3 B:GOL1503 4.6 20.4 0.5 OG B:SER221 4.7 8.0 0.3 O2 B:GOL1503 4.7 20.6 0.5 O1 B:GOL1503 4.8 19.9 0.5 OD1 B:ASP120 4.9 8.2 1.0 CG2 B:THR197 4.9 5.8 1.0 CA B:HIS118 4.9 6.4 1.0

Zinc binding site 4 out of 4 in the Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Native Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn4 b:10.9 occ:1.00 OD1 B:ASP120 2.1 8.2 1.0 NE2 B:HIS121 2.1 5.9 1.0 NE2 B:HIS263 2.1 7.0 1.0 O2 B:GOL1503 2.2 18.9 0.5 O1 B:GOL1503 2.3 19.9 0.5 O B:HOH1565 2.3 4.3 0.5 O3 B:GOL1503 2.6 19.9 0.5 C2 B:GOL1503 2.9 19.4 0.5 C3 B:GOL1503 2.9 20.4 0.5 C1 B:GOL1503 3.0 19.8 0.5 CE1 B:HIS121 3.0 6.6 1.0 CG B:ASP120 3.0 8.1 1.0 CE1 B:HIS263 3.0 8.2 1.0 CD2 B:HIS121 3.1 6.7 1.0 CD2 B:HIS263 3.1 7.7 1.0 OD2 B:ASP120 3.2 8.0 1.0 C1 B:GOL1503 3.4 20.2 0.5 ZN B:ZN3 3.7 8.2 1.0 C2 B:GOL1503 3.8 19.7 0.5 NE2 B:HIS116 4.0 5.9 1.0 CE1 B:HIS116 4.1 5.4 1.0 ND1 B:HIS121 4.1 6.4 1.0 CG B:HIS121 4.2 6.1 1.0 ND1 B:HIS263 4.2 7.2 1.0 CG B:HIS263 4.2 7.2 1.0 O B:HOH1565 4.3 6.5 0.5 C3 B:GOL1503 4.3 19.6 0.5 CB B:ASP120 4.4 7.7 1.0 O3 B:GOL1503 4.6 19.3 0.5 O1 B:GOL1503 4.7 19.9 0.5 O2 B:GOL1503 4.8 20.6 0.5 OG B:SER262 5.0 6.9 1.0 NE2 B:HIS196 5.0 5.4 1.0

I.Garcia-Saez, P.S.Mercuri, C.Papamicael, R.Kahn, J.M.Frere, M.Galleni, G.M.Rossolini, O.Dideberg. Three-Dimensional Structure of Fez-1, A Monomeric Subclass B3 Metallo-[Beta]-Lactamase From Fluoribacter Gormanii, in Native Form and in Complex with -Captopril J.Mol.Biol. V. 325 651 2003.
ISSN: ISSN 0022-2836
PubMed: 12507470
DOI: 10.1016/S0022-2836(02)01271-8