Atomistry » Zinc » PDB 1d5j-1dmy » 1dd6
Atomistry »
  Zinc »
    PDB 1d5j-1dmy »
      1dd6 »

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

Go back to Zinc Binding Sites List in 1dd6
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

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy