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Zinc in PDB 1dd6: Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Mercaptocarboxylate Inhibitor

Enzymatic activity of Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Mercaptocarboxylate Inhibitor

All present enzymatic activity of Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Mercaptocarboxylate Inhibitor:
3.5.2.6;

Protein crystallography data

The structure of Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Mercaptocarboxylate Inhibitor, PDB code: 1dd6 was solved by N.O.Concha, C.A.Janson, P.Rowling, S.Pearson, C.A.Cheever, B.P.Clarke, C.Lewis, M.Galleni, J.M.Frere, D.J.Payne, J.H.Bateson, S.S.Abdel-Meguid, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 49.300, 51.200, 203.300, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 25.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Mercaptocarboxylate Inhibitor (pdb code 1dd6). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Mercaptocarboxylate Inhibitor, PDB code: 1dd6:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 1dd6

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Zinc binding site 1 out of 4 in the Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Mercaptocarboxylate Inhibitor


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 Mercaptocarboxylate Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn502

b:23.3
occ:1.00
 ND1 A:HIS79 2.2 25.6 1.0
NE2 A:HIS139 2.2 16.6 1.0
NE2 A:HIS77 2.2 19.7 1.0
S20 A:MCI550 2.2 23.6 1.0
CD2 A:HIS77 3.0 20.3 1.0
CD2 A:HIS139 3.1 18.8 1.0
CG A:HIS79 3.1 23.6 1.0
CE1 A:HIS79 3.1 19.6 1.0
CE1 A:HIS139 3.2 24.8 1.0
CE1 A:HIS77 3.3 30.6 1.0
CB A:HIS79 3.4 14.9 1.0
C19 A:MCI550 3.5 30.8 1.0
ZN A:ZN503 3.6 24.9 1.0
CB A:CYS158 4.0 19.0 1.0
OD1 A:ASP81 4.1 17.6 1.0
SG A:CYS158 4.1 21.5 1.0
NE2 A:HIS79 4.2 23.8 1.0
CG A:HIS77 4.2 19.0 1.0
CD2 A:HIS79 4.2 12.4 1.0
CG A:HIS139 4.2 23.0 1.0
ND1 A:HIS139 4.3 22.0 1.0
CG2 A:THR140 4.3 16.3 1.0
ND1 A:HIS77 4.3 16.3 1.0
O30 A:MCI550 4.4 30.2 1.0
OD2 A:ASP81 4.7 21.6 1.0
CA A:HIS79 4.8 18.1 1.0
C16 A:MCI550 4.8 27.5 1.0
CG A:ASP81 4.8 17.5 1.0
C28 A:MCI550 4.9 36.8 1.0
N A:HIS79 5.0 19.6 1.0
O A:HOH654 5.0 38.5 1.0

Zinc binding site 2 out of 4 in 1dd6

Go back to Zinc Binding Sites List in 1dd6
Zinc binding site 2 out of 4 in the Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Mercaptocarboxylate Inhibitor


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 Mercaptocarboxylate Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn503

b:24.9
occ:1.00
 OD2 A:ASP81 2.1 21.6 1.0
NE2 A:HIS197 2.3 20.2 1.0
SG A:CYS158 2.3 21.5 1.0
S20 A:MCI550 2.4 23.6 1.0
CG A:ASP81 3.0 17.5 1.0
CE1 A:HIS197 3.1 23.3 1.0
CD2 A:HIS197 3.3 23.4 1.0
C19 A:MCI550 3.3 30.8 1.0
OD1 A:ASP81 3.3 17.6 1.0
CB A:CYS158 3.4 19.0 1.0
O30 A:MCI550 3.6 30.2 1.0
ZN A:ZN502 3.6 23.3 1.0
C16 A:MCI550 3.9 27.5 1.0
CE1 A:HIS77 4.1 30.6 1.0
NE2 A:HIS77 4.1 19.7 1.0
ND1 A:HIS197 4.2 18.1 1.0
C27 A:MCI550 4.3 42.0 1.0
CB A:ASP81 4.4 17.7 1.0
CG A:HIS197 4.4 21.1 1.0
C28 A:MCI550 4.4 36.8 1.0
CE A:LYS33 4.4 17.6 1.0
CD A:LYS33 4.5 14.3 1.0
CB A:SER196 4.5 18.0 1.0
CA A:CYS158 4.6 21.6 1.0
NE2 A:HIS139 4.6 16.6 1.0
OG A:SER196 4.7 18.7 1.0
C23 A:MCI550 4.8 37.6 1.0
N26 A:MCI550 4.9 43.0 1.0

Zinc binding site 3 out of 4 in 1dd6

Go back to Zinc Binding Sites List in 1dd6
Zinc binding site 3 out of 4 in the Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Mercaptocarboxylate Inhibitor


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 Mercaptocarboxylate Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn504

b:31.4
occ:1.00
 NE2 B:HIS139 2.2 27.4 1.0
ND1 B:HIS79 2.2 31.7 1.0
NE2 B:HIS77 2.3 28.9 1.0
S20 B:MCI551 2.4 39.0 1.0
CD2 B:HIS77 3.0 25.4 1.0
CG B:HIS79 3.1 32.7 1.0
CE1 B:HIS139 3.1 35.1 1.0
CD2 B:HIS139 3.2 30.9 1.0
CE1 B:HIS79 3.2 33.5 1.0
CB B:HIS79 3.3 22.4 1.0
CE1 B:HIS77 3.5 27.0 1.0
ZN B:ZN505 3.6 36.7 1.0
C19 B:MCI551 3.8 38.2 1.0
OD1 B:ASP81 4.0 30.4 1.0
CB B:CYS158 4.0 31.5 1.0
SG B:CYS158 4.1 30.9 1.0
CD2 B:HIS79 4.2 32.6 1.0
ND1 B:HIS139 4.2 38.0 1.0
CG B:HIS77 4.3 29.8 1.0
CG B:HIS139 4.3 32.9 1.0
NE2 B:HIS79 4.3 35.0 1.0
CG2 B:THR140 4.4 31.2 1.0
ND1 B:HIS77 4.5 28.2 1.0
CA B:HIS79 4.7 30.0 1.0
OD2 B:ASP81 4.8 36.4 1.0
O30 B:MCI551 4.8 39.6 1.0
CG B:ASP81 4.8 35.4 1.0

Zinc binding site 4 out of 4 in 1dd6

Go back to Zinc Binding Sites List in 1dd6
Zinc binding site 4 out of 4 in the Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa in Complex with A Mercaptocarboxylate Inhibitor


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 Mercaptocarboxylate Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn505

b:36.7
occ:1.00
 OD2 B:ASP81 2.2 36.4 1.0
SG B:CYS158 2.4 30.9 1.0
NE2 B:HIS197 2.4 38.3 1.0
S20 B:MCI551 2.6 39.0 1.0
CG B:ASP81 3.1 35.4 1.0
CD2 B:HIS197 3.3 38.1 1.0
OD1 B:ASP81 3.3 30.4 1.0
CB B:CYS158 3.4 31.5 1.0
CE1 B:HIS197 3.4 41.7 1.0
C19 B:MCI551 3.6 38.2 1.0
ZN B:ZN504 3.6 31.4 1.0
O30 B:MCI551 3.7 39.6 1.0
C16 B:MCI551 3.9 48.6 1.0
NE2 B:HIS77 4.1 28.9 1.0
CE1 B:HIS77 4.2 27.0 1.0
CD B:LYS33 4.3 30.2 1.0
C27 B:MCI551 4.4 52.0 1.0
CG B:HIS197 4.4 40.0 1.0
CB B:ASP81 4.4 29.6 1.0
C28 B:MCI551 4.4 47.6 1.0
CB B:SER196 4.5 31.7 1.0
ND1 B:HIS197 4.5 35.3 1.0
CE B:LYS33 4.5 28.6 1.0
N26 B:MCI551 4.6 52.6 1.0
CA B:CYS158 4.6 32.9 1.0
NE2 B:HIS139 4.6 27.4 1.0
OG B:SER196 4.8 32.6 1.0
C23 B:MCI551 4.8 49.5 1.0

Reference:

N.O.Concha, C.A.Janson, P.Rowling, S.Pearson, C.A.Cheever, B.P.Clarke, C.Lewis, M.Galleni, J.M.Frere, D.J.Payne, J.H.Bateson, S.S.Abdel-Meguid. Crystal Structure of the Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa and Its Complex with A Mercaptocarboxylate Inhibitor: Binding Determinants of A Potent, Broad-Spectrum Inhibitor. Biochemistry V. 39 4288 2000.
ISSN: ISSN 0006-2960
PubMed: 10757977
DOI: 10.1021/BI992569M
Page generated: Sat Oct 12 23:37:30 2024

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