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: Mon Jan 25 16:08:19 2021

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy