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Zinc in PDB 1jje: Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Biaryl Succinic Acid Inhibitor (11)

Enzymatic activity of Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Biaryl Succinic Acid Inhibitor (11)

All present enzymatic activity of Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Biaryl Succinic Acid Inhibitor (11):
3.5.2.6;

Protein crystallography data

The structure of Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Biaryl Succinic Acid Inhibitor (11), PDB code: 1jje was solved by P.M.D.Fitzgerald, N.Sharma, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 71.440, 43.240, 64.230, 90.00, 100.93, 90.00
R / Rfree (%) 20.1 / 29.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Biaryl Succinic Acid Inhibitor (11) (pdb code 1jje). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Biaryl Succinic Acid Inhibitor (11), PDB code: 1jje:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in 1jje

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Zinc binding site 1 out of 6 in the Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Biaryl Succinic Acid Inhibitor (11)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Biaryl Succinic Acid Inhibitor (11) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn251

b:21.9
occ:1.00
 NE2 A:HIS139 2.0 19.6 1.0
O3 A:BYS250 2.0 21.6 1.0
ND1 A:HIS79 2.1 23.7 1.0
NE2 A:HIS77 2.1 17.8 1.0
O4 A:BYS250 2.7 19.8 1.0
C2 A:BYS250 2.7 16.5 1.0
CE1 A:HIS139 3.0 19.0 1.0
CG A:HIS79 3.0 22.7 1.0
CD2 A:HIS139 3.0 17.0 1.0
CD2 A:HIS77 3.0 18.9 1.0
CE1 A:HIS79 3.0 25.2 1.0
CE1 A:HIS77 3.1 20.5 1.0
CB A:HIS79 3.3 21.0 1.0
ZN A:ZN252 3.6 20.7 1.0
OD1 A:ASP81 3.9 23.5 1.0
SG A:CYS158 3.9 20.8 1.0
CB A:CYS158 4.1 22.5 1.0
O14 A:BYS250 4.1 26.0 1.0
ND1 A:HIS139 4.1 24.5 1.0
CD2 A:HIS79 4.1 31.5 1.0
CG A:HIS139 4.1 24.6 1.0
NE2 A:HIS79 4.1 32.9 1.0
C1 A:BYS250 4.2 24.3 1.0
CG A:HIS77 4.2 18.6 1.0
ND1 A:HIS77 4.2 19.5 1.0
OD2 A:ASP81 4.4 23.8 1.0
CG A:ASP81 4.6 21.9 1.0
C13 A:BYS250 4.6 23.8 1.0
CG2 A:THR140 4.6 19.9 1.0
CA A:HIS79 4.7 18.3 1.0
C7 A:BYS250 4.8 26.8 1.0
C6 A:BYS250 4.9 25.4 1.0

Zinc binding site 2 out of 6 in 1jje

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Zinc binding site 2 out of 6 in the Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Biaryl Succinic Acid Inhibitor (11)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Biaryl Succinic Acid Inhibitor (11) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn252

b:20.7
occ:1.00
 OD2 A:ASP81 2.0 23.8 1.0
O3 A:BYS250 2.1 21.6 1.0
NE2 A:HIS197 2.2 21.8 1.0
SG A:CYS158 2.3 20.8 1.0
O14 A:BYS250 2.3 26.0 1.0
C2 A:BYS250 2.9 16.5 1.0
CG A:ASP81 3.1 21.9 1.0
CD2 A:HIS197 3.1 23.7 1.0
CE1 A:HIS197 3.1 15.4 1.0
C1 A:BYS250 3.2 24.3 1.0
C13 A:BYS250 3.3 23.8 1.0
CB A:CYS158 3.4 22.5 1.0
OD1 A:ASP81 3.5 23.5 1.0
ZN A:ZN251 3.6 21.9 1.0
C12 A:BYS250 3.7 19.9 1.0
O4 A:BYS250 4.0 19.8 1.0
C16 A:BYS250 4.2 19.7 1.0
ND1 A:HIS197 4.2 19.4 1.0
CG A:HIS197 4.3 17.4 1.0
NE2 A:HIS139 4.3 19.6 1.0
CE1 A:HIS77 4.4 20.5 1.0
NE2 A:HIS77 4.4 17.8 1.0
O15 A:BYS250 4.4 26.0 1.0
CB A:SER196 4.4 19.1 1.0
CB A:ASP81 4.4 19.1 1.0
CA A:CYS158 4.5 19.4 1.0
C5 A:BYS250 4.6 19.7 1.0
CE1 A:HIS139 4.6 19.0 1.0
OG A:SER196 4.6 18.2 1.0
CD A:LYS33 4.7 16.2 1.0
CE A:LYS33 4.8 18.8 1.0
C6 A:BYS250 4.9 25.4 1.0
C11 A:BYS250 5.0 30.9 1.0

Zinc binding site 3 out of 6 in 1jje

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Zinc binding site 3 out of 6 in the Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Biaryl Succinic Acid Inhibitor (11)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Biaryl Succinic Acid Inhibitor (11) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn261

b:21.9
occ:1.00
 O A:ACT260 1.8 47.5 1.0
O A:HOH1031 2.1 28.4 1.0
NE2 A:HIS34 2.1 21.9 1.0
OE2 A:GLU199 2.3 25.0 1.0
OE1 A:GLU199 2.4 20.2 1.0
C A:ACT260 2.5 22.4 1.0
OXT A:ACT260 2.6 41.3 1.0
CD A:GLU199 2.7 25.9 1.0
CE1 A:HIS34 3.0 23.8 1.0
CD2 A:HIS34 3.1 18.1 1.0
OG1 A:THR20 3.9 21.8 1.0
CH3 A:ACT260 4.0 22.1 1.0
CG2 A:THR20 4.1 28.1 1.0
NZ A:LYS8 4.1 18.1 1.0
ND1 A:HIS34 4.2 24.3 1.0
CG A:GLU199 4.2 16.8 1.0
CG A:HIS34 4.2 21.3 1.0
OE1 A:GLU10 4.6 43.0 1.0
CB A:THR20 4.6 22.3 1.0
O A:HOH1034 4.7 28.9 1.0

Zinc binding site 4 out of 6 in 1jje

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Zinc binding site 4 out of 6 in the Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Biaryl Succinic Acid Inhibitor (11)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Biaryl Succinic Acid Inhibitor (11) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn251

b:24.3
occ:1.00
 NE2 B:HIS139 2.0 17.9 1.0
O3 B:BYS250 2.0 25.1 1.0
ND1 B:HIS79 2.1 24.8 1.0
NE2 B:HIS77 2.1 24.3 1.0
O4 B:BYS250 2.7 21.5 1.0
C2 B:BYS250 2.7 24.4 1.0
CD2 B:HIS139 2.9 15.3 1.0
CE1 B:HIS139 3.0 25.0 1.0
CG B:HIS79 3.1 26.9 1.0
CE1 B:HIS79 3.1 21.9 1.0
CD2 B:HIS77 3.1 30.0 1.0
CE1 B:HIS77 3.1 31.0 1.0
CB B:HIS79 3.4 29.0 1.0
ZN B:ZN252 3.6 21.3 1.0
OD1 B:ASP81 3.9 24.7 1.0
SG B:CYS158 3.9 21.3 1.0
O14 B:BYS250 4.0 27.7 1.0
CG B:HIS139 4.1 20.2 1.0
ND1 B:HIS139 4.1 22.1 1.0
CB B:CYS158 4.1 25.1 1.0
NE2 B:HIS79 4.2 23.0 1.0
CD2 B:HIS79 4.2 21.8 1.0
ND1 B:HIS77 4.2 35.2 1.0
C1 B:BYS250 4.2 18.9 1.0
CG B:HIS77 4.2 26.0 1.0
OD2 B:ASP81 4.5 19.7 1.0
CG2 B:THR140 4.5 29.4 1.0
C13 B:BYS250 4.5 27.2 1.0
CG B:ASP81 4.6 27.5 1.0
CA B:HIS79 4.8 21.4 1.0
C7 B:BYS250 4.9 24.1 1.0
C6 B:BYS250 4.9 21.0 1.0

Zinc binding site 5 out of 6 in 1jje

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Zinc binding site 5 out of 6 in the Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Biaryl Succinic Acid Inhibitor (11)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Biaryl Succinic Acid Inhibitor (11) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn252

b:21.3
occ:1.00
 OD2 B:ASP81 2.0 19.7 1.0
O3 B:BYS250 2.1 25.1 1.0
NE2 B:HIS197 2.1 27.2 1.0
SG B:CYS158 2.3 21.3 1.0
O14 B:BYS250 2.3 27.7 1.0
C2 B:BYS250 2.9 24.4 1.0
CG B:ASP81 3.1 27.5 1.0
CD2 B:HIS197 3.1 21.2 1.0
CE1 B:HIS197 3.1 25.0 1.0
C1 B:BYS250 3.2 18.9 1.0
C13 B:BYS250 3.4 27.2 1.0
CB B:CYS158 3.4 25.1 1.0
OD1 B:ASP81 3.5 24.7 1.0
ZN B:ZN251 3.6 24.3 1.0
C12 B:BYS250 3.8 21.3 1.0
O4 B:BYS250 4.0 21.5 1.0
C16 B:BYS250 4.2 24.7 1.0
ND1 B:HIS197 4.2 21.5 1.0
CG B:HIS197 4.3 26.3 1.0
CE1 B:HIS77 4.3 31.0 1.0
NE2 B:HIS139 4.3 17.9 1.0
NE2 B:HIS77 4.4 24.3 1.0
CB B:ASP81 4.4 19.6 1.0
CB B:SER196 4.5 19.5 1.0
O15 B:BYS250 4.5 21.4 1.0
CA B:CYS158 4.6 21.5 1.0
C5 B:BYS250 4.6 22.3 1.0
C11 B:BYS250 4.7 19.4 1.0
CD B:LYS33 4.7 13.4 1.0
OG B:SER196 4.8 19.2 1.0
CE1 B:HIS139 4.8 25.0 1.0
C6 B:BYS250 4.8 21.0 1.0
CE B:LYS33 4.9 14.6 1.0

Zinc binding site 6 out of 6 in 1jje

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Zinc binding site 6 out of 6 in the Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Biaryl Succinic Acid Inhibitor (11)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Biaryl Succinic Acid Inhibitor (11) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn261

b:20.6
occ:1.00
 O B:ACT260 1.9 30.4 1.0
O B:HOH1019 1.9 23.9 1.0
NE2 B:HIS34 2.1 25.3 1.0
OE2 B:GLU199 2.2 30.4 1.0
OE1 B:GLU199 2.3 22.1 1.0
C B:ACT260 2.6 20.1 1.0
CD B:GLU199 2.6 24.8 1.0
OXT B:ACT260 2.7 38.7 1.0
CD2 B:HIS34 3.0 29.6 1.0
CE1 B:HIS34 3.1 38.0 1.0
O B:HOH1044 3.3 31.8 1.0
CH3 B:ACT260 4.1 21.9 1.0
OG1 B:THR20 4.1 19.6 1.0
CG B:GLU199 4.2 24.6 1.0
ND1 B:HIS34 4.2 30.8 1.0
CG B:HIS34 4.2 23.9 1.0
CG2 B:THR20 4.5 25.0 1.0
OE1 B:GLU10 4.7 35.4 1.0
CB B:THR20 4.9 24.1 1.0

Reference:

J.H.Toney, G.G.Hammond, P.M.Fitzgerald, N.Sharma, J.M.Balkovec, G.P.Rouen, S.H.Olson, M.L.Hammond, M.L.Greenlee, Y.D.Gao. Succinic Acids As Potent Inhibitors of Plasmid-Borne Imp-1 Metallo-Beta-Lactamase. J.Biol.Chem. V. 276 31913 2001.
ISSN: ISSN 0021-9258
PubMed: 11390410
DOI: 10.1074/JBC.M104742200
Page generated: Sun Oct 13 03:35:06 2024

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