Atomistry » Zinc » PDB 2wfq-2wwn » 2wrs
Atomistry »
  Zinc »
    PDB 2wfq-2wwn »
      2wrs »

Zinc in PDB 2wrs: Crystal Structure of the Mono-Zinc Metallo-Beta-Lactamase Vim-4 From Pseudomonas Aeruginosa

Enzymatic activity of Crystal Structure of the Mono-Zinc Metallo-Beta-Lactamase Vim-4 From Pseudomonas Aeruginosa

All present enzymatic activity of Crystal Structure of the Mono-Zinc Metallo-Beta-Lactamase Vim-4 From Pseudomonas Aeruginosa:
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of the Mono-Zinc Metallo-Beta-Lactamase Vim-4 From Pseudomonas Aeruginosa, PDB code: 2wrs was solved by P.Lassaux, M.Hamel, M.Gulea, H.Delbruck, D.A.K.Traore, P.S.Mercuri, L.Horsfall, D.Dehareng, A.-C.Gaumont, J.-M.Frere, J.-L.Ferrer, K.Hoffmann, M.Galleni, C.Bebrone, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.27 / 2.79
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 140.130, 45.670, 105.030, 90.00, 105.41, 90.00
R / Rfree (%) 19.861 / 25.318

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Mono-Zinc Metallo-Beta-Lactamase Vim-4 From Pseudomonas Aeruginosa (pdb code 2wrs). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Mono-Zinc Metallo-Beta-Lactamase Vim-4 From Pseudomonas Aeruginosa, PDB code: 2wrs:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2wrs

Go back to Zinc Binding Sites List in 2wrs
Zinc binding site 1 out of 2 in the Crystal Structure of the Mono-Zinc Metallo-Beta-Lactamase Vim-4 From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Mono-Zinc Metallo-Beta-Lactamase Vim-4 From Pseudomonas Aeruginosa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1262

b:38.3
occ:1.00
ND1 A:HIS116 2.1 30.7 1.0
NE2 A:HIS179 2.1 24.9 1.0
OB2 A:FLC1263 2.2 58.4 1.0
NE2 A:HIS114 2.3 23.1 1.0
CG A:HIS116 2.9 28.9 1.0
CE1 A:HIS179 3.0 25.9 1.0
CE1 A:HIS116 3.1 31.6 1.0
CD2 A:HIS114 3.2 23.8 1.0
CB A:HIS116 3.2 25.6 1.0
CBC A:FLC1263 3.2 60.0 1.0
OHB A:FLC1263 3.3 62.1 1.0
CD2 A:HIS179 3.3 23.6 1.0
CE1 A:HIS114 3.3 23.8 1.0
CB A:FLC1263 3.9 61.9 1.0
OD1 A:ASP118 3.9 26.8 1.0
CD2 A:HIS116 4.1 29.7 1.0
SG A:CYS198 4.1 29.5 1.0
OB1 A:FLC1263 4.1 55.5 1.0
NE2 A:HIS116 4.1 31.4 1.0
ND1 A:HIS179 4.2 24.6 1.0
CAC A:FLC1263 4.3 63.5 1.0
CG A:HIS179 4.3 21.6 1.0
CB A:CYS198 4.4 27.7 1.0
ND1 A:HIS114 4.4 24.4 1.0
CG A:HIS114 4.4 20.8 1.0
OA2 A:FLC1263 4.4 63.2 1.0
OD2 A:ASP118 4.4 29.2 1.0
OA1 A:FLC1263 4.5 64.7 1.0
CG A:ASP118 4.6 27.9 1.0
CA A:HIS116 4.7 25.7 1.0
CA A:FLC1263 4.7 62.6 1.0
ND2 A:ASN210 5.0 52.9 1.0

Zinc binding site 2 out of 2 in 2wrs

Go back to Zinc Binding Sites List in 2wrs
Zinc binding site 2 out of 2 in the Crystal Structure of the Mono-Zinc Metallo-Beta-Lactamase Vim-4 From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Mono-Zinc Metallo-Beta-Lactamase Vim-4 From Pseudomonas Aeruginosa within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1262

b:58.5
occ:1.00
ND1 B:HIS116 1.9 49.0 1.0
OG2 B:FLC1263 2.1 70.9 1.0
NE2 B:HIS179 2.3 59.0 1.0
NE2 B:HIS114 2.7 51.1 1.0
CG B:HIS116 2.8 48.4 1.0
OB1 B:FLC1263 2.9 71.8 1.0
CE1 B:HIS116 3.0 49.0 1.0
CE1 B:HIS179 3.1 59.6 1.0
CB B:HIS116 3.1 46.9 1.0
CGC B:FLC1263 3.2 70.9 1.0
CD2 B:HIS179 3.4 60.0 1.0
CE1 B:HIS114 3.5 50.5 1.0
CD2 B:HIS114 3.7 49.5 1.0
CBC B:FLC1263 3.7 71.1 1.0
OD1 B:ASP118 3.9 46.9 1.0
SG B:CYS198 3.9 57.9 1.0
CD2 B:HIS116 4.0 49.0 1.0
NE2 B:HIS116 4.0 49.7 1.0
OG1 B:FLC1263 4.1 71.0 1.0
CB B:CYS198 4.1 57.5 1.0
CG B:FLC1263 4.1 70.8 1.0
OA1 B:FLC1263 4.2 69.5 1.0
ND1 B:HIS179 4.3 60.4 1.0
CB B:FLC1263 4.4 71.0 1.0
CAC B:FLC1263 4.4 69.6 1.0
CG B:HIS179 4.5 60.1 1.0
OB2 B:FLC1263 4.5 70.1 1.0
CA B:HIS116 4.6 47.0 1.0
ND1 B:HIS114 4.6 49.4 1.0
OD2 B:ASP118 4.7 46.3 1.0
CG B:ASP118 4.7 46.3 1.0
CA B:FLC1263 4.7 70.4 1.0
CG B:HIS114 4.7 47.6 1.0
OA2 B:FLC1263 4.8 69.4 1.0
N B:HIS116 4.9 46.6 1.0

Reference:

P.Lassaux, M.Hamel, M.Gulea, H.Delbruck, P.S.Mercuri, L.Horsfall, D.Dehareng, M.Kupper, J.-M.Frere, K.Hoffmann, M.Galleni, C.Bebrone. Mercaptophosphonate Compounds As Broad-Spectrum Inhibitors of the Metallo-Beta-Lactamases. J.Med.Chem. V. 53 4862 2010.
ISSN: ISSN 0022-2623
PubMed: 20527888
DOI: 10.1021/JM100213C
Page generated: Wed Dec 16 03:58:21 2020

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