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Zinc in PDB 1l9y: Fez-1-Y228A, A Mutant of the Metallo-Beta-Lactamase From Legionella Gormanii

Enzymatic activity of Fez-1-Y228A, A Mutant of the Metallo-Beta-Lactamase From Legionella Gormanii

All present enzymatic activity of Fez-1-Y228A, A Mutant of the Metallo-Beta-Lactamase From Legionella Gormanii:
3.5.2.6;

Protein crystallography data

The structure of Fez-1-Y228A, A Mutant of the Metallo-Beta-Lactamase From Legionella Gormanii, PDB code: 1l9y was solved by I.Garcia-Saez, P.S.Mercuri, 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 / 2.01
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 44.761, 77.430, 78.499, 90.00, 101.70, 90.00
R / Rfree (%) 18.6 / 21.6

Other elements in 1l9y:

The structure of Fez-1-Y228A, A Mutant of the Metallo-Beta-Lactamase From Legionella Gormanii also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Fez-1-Y228A, A Mutant of the Metallo-Beta-Lactamase From Legionella Gormanii (pdb code 1l9y). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Fez-1-Y228A, A Mutant of the Metallo-Beta-Lactamase From Legionella Gormanii, PDB code: 1l9y:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 1l9y

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Zinc binding site 1 out of 4 in the Fez-1-Y228A, A Mutant of the 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 Fez-1-Y228A, A Mutant of the Metallo-Beta-Lactamase From Legionella Gormanii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1

b:17.7
occ:1.00
 NE2 A:HIS196 2.1 9.2 1.0
ND1 A:HIS118 2.2 12.6 1.0
NE2 A:HIS116 2.3 8.8 1.0
O4 A:SO4501 2.3 20.1 1.0
CD2 A:HIS196 2.9 8.6 1.0
CE1 A:HIS118 3.1 12.5 1.0
CE1 A:HIS116 3.1 9.2 1.0
CG A:HIS118 3.2 12.6 1.0
CD2 A:HIS116 3.2 8.4 1.0
CE1 A:HIS196 3.3 9.1 1.0
S A:SO4501 3.5 17.6 1.0
O A:HOH645 3.5 12.4 0.5
CB A:HIS118 3.6 11.9 1.0
O3 A:SO4501 3.6 20.1 1.0
ZN A:ZN2 3.6 22.0 1.0
CG A:HIS196 4.1 9.3 1.0
ND1 A:HIS116 4.2 8.4 1.0
NE2 A:HIS118 4.2 13.3 1.0
ND1 A:HIS196 4.3 8.8 1.0
ND2 A:ASN225 4.3 18.2 1.0
O1 A:SO4501 4.3 21.4 1.0
CG A:HIS116 4.3 8.4 1.0
CD2 A:HIS118 4.3 12.7 1.0
OD2 A:ASP120 4.4 15.1 1.0
CD2 A:HIS121 4.4 9.0 1.0
O A:HOH645 4.5 5.2 0.5
O2 A:SO4501 4.5 21.8 1.0
NE2 A:HIS121 4.6 8.2 1.0
OD1 A:ASP120 4.9 14.0 1.0
CG2 A:THR197 5.0 9.4 1.0
OD1 A:ASN225 5.0 18.1 1.0

Zinc binding site 2 out of 4 in 1l9y

Go back to Zinc Binding Sites List in 1l9y
Zinc binding site 2 out of 4 in the Fez-1-Y228A, A Mutant of the 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 Fez-1-Y228A, A Mutant of the Metallo-Beta-Lactamase From Legionella Gormanii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn2

b:22.0
occ:1.00
 NE2 A:HIS263 2.2 9.7 1.0
NE2 A:HIS121 2.2 8.2 1.0
OD1 A:ASP120 2.2 14.0 1.0
O3 A:SO4501 2.2 20.1 1.0
O A:HOH645 2.7 12.4 0.5
CD2 A:HIS121 3.1 9.0 1.0
CD2 A:HIS263 3.1 9.8 1.0
CG A:ASP120 3.1 13.9 1.0
CE1 A:HIS121 3.1 8.7 1.0
CE1 A:HIS263 3.2 10.6 1.0
OD2 A:ASP120 3.4 15.1 1.0
S A:SO4501 3.5 17.6 1.0
ZN A:ZN1 3.6 17.7 1.0
O A:HOH645 3.8 5.2 0.5
O4 A:SO4501 3.8 20.1 1.0
CE1 A:HIS116 4.0 9.2 1.0
NE2 A:HIS116 4.1 8.8 1.0
O1 A:SO4501 4.1 21.4 1.0
ND1 A:HIS121 4.2 8.2 1.0
CG A:HIS121 4.2 9.2 1.0
ND1 A:HIS263 4.3 10.1 1.0
CG A:HIS263 4.3 10.4 1.0
CB A:ASP120 4.5 13.1 1.0
O2 A:SO4501 4.6 21.8 1.0
NE2 A:HIS196 5.0 9.2 1.0

Zinc binding site 3 out of 4 in 1l9y

Go back to Zinc Binding Sites List in 1l9y
Zinc binding site 3 out of 4 in the Fez-1-Y228A, A Mutant of the 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 Fez-1-Y228A, A Mutant of the Metallo-Beta-Lactamase From Legionella Gormanii within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1

b:17.8
occ:1.00
 NE2 B:HIS196 2.2 8.5 1.0
ND1 B:HIS118 2.2 12.6 1.0
NE2 B:HIS116 2.3 10.0 1.0
O2 B:SO4503 2.3 19.5 1.0
CD2 B:HIS196 2.9 7.7 1.0
CE1 B:HIS118 3.1 12.7 1.0
CD2 B:HIS116 3.1 9.4 1.0
CG B:HIS118 3.2 12.1 1.0
CE1 B:HIS116 3.2 9.4 1.0
CE1 B:HIS196 3.3 9.0 1.0
S B:SO4503 3.5 15.7 1.0
CB B:HIS118 3.5 11.4 1.0
ZN B:ZN2 3.6 19.9 1.0
O B:HOH663 3.6 20.2 0.5
O3 B:SO4503 3.7 18.7 1.0
CG B:HIS196 4.2 9.1 1.0
O4 B:SO4503 4.2 20.7 1.0
NE2 B:HIS118 4.3 12.6 1.0
CG B:HIS116 4.3 9.5 1.0
CD2 B:HIS121 4.3 10.6 1.0
ND1 B:HIS116 4.3 9.7 1.0
ND1 B:HIS196 4.3 8.1 1.0
OD2 B:ASP120 4.3 15.4 1.0
CD2 B:HIS118 4.3 12.5 1.0
ND2 B:ASN225 4.4 18.8 1.0
NE2 B:HIS121 4.4 10.3 1.0
O1 B:SO4503 4.6 20.7 1.0
O B:HOH663 4.6 2.2 0.5
OD1 B:ASP120 4.8 14.5 1.0
CG2 B:THR197 5.0 10.5 1.0

Zinc binding site 4 out of 4 in 1l9y

Go back to Zinc Binding Sites List in 1l9y
Zinc binding site 4 out of 4 in the Fez-1-Y228A, A Mutant of the 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 Fez-1-Y228A, A Mutant of the Metallo-Beta-Lactamase From Legionella Gormanii within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn2

b:19.9
occ:1.00
 NE2 B:HIS121 2.2 10.3 1.0
NE2 B:HIS263 2.2 10.4 1.0
OD1 B:ASP120 2.2 14.5 1.0
O3 B:SO4503 2.3 18.7 1.0
O B:HOH663 2.9 20.2 0.5
CE1 B:HIS121 3.1 11.2 1.0
CD2 B:HIS121 3.1 10.6 1.0
CG B:ASP120 3.1 14.0 1.0
CD2 B:HIS263 3.1 10.2 1.0
CE1 B:HIS263 3.2 10.5 1.0
OD2 B:ASP120 3.3 15.4 1.0
S B:SO4503 3.4 15.7 1.0
ZN B:ZN1 3.6 17.8 1.0
O2 B:SO4503 3.7 19.5 1.0
O4 B:SO4503 3.8 20.7 1.0
NE2 B:HIS116 4.0 10.0 1.0
CE1 B:HIS116 4.1 9.4 1.0
ND1 B:HIS121 4.1 11.2 1.0
CG B:HIS121 4.2 11.4 1.0
O B:HOH663 4.3 2.2 0.5
CG B:HIS263 4.3 10.6 1.0
ND1 B:HIS263 4.3 10.6 1.0
CB B:ASP120 4.5 13.3 1.0
O1 B:SO4503 4.6 20.7 1.0
OG B:SER262 4.9 12.1 1.0
NE2 B:HIS196 5.0 8.5 1.0

Reference:

I.Garcia-Saez, P.S.Mercuri, C.Papamicael, R.Kahn, J.M.Frre, 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
Page generated: Sun Oct 13 04:52:09 2024

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