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Zinc in PDB 4nq2: Structure of Zn(II)-Bound Metallo-Beta-Lactamse Vim-2 From Pseudomonas Aeruginosa

Enzymatic activity of Structure of Zn(II)-Bound Metallo-Beta-Lactamse Vim-2 From Pseudomonas Aeruginosa

All present enzymatic activity of Structure of Zn(II)-Bound Metallo-Beta-Lactamse Vim-2 From Pseudomonas Aeruginosa:
3.5.2.6;

Protein crystallography data

The structure of Structure of Zn(II)-Bound Metallo-Beta-Lactamse Vim-2 From Pseudomonas Aeruginosa, PDB code: 4nq2 was solved by M.Aitha, J.C.Nix, M.W.Crowder, R.C.Page, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 55.87 / 1.55
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 68.294, 78.266, 79.767, 90.00, 90.00, 90.00
R / Rfree (%) 17.6 / 20.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Zn(II)-Bound Metallo-Beta-Lactamse Vim-2 From Pseudomonas Aeruginosa (pdb code 4nq2). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Structure of Zn(II)-Bound Metallo-Beta-Lactamse Vim-2 From Pseudomonas Aeruginosa, PDB code: 4nq2:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in 4nq2

Go back to Zinc Binding Sites List in 4nq2
Zinc binding site 1 out of 3 in the Structure of Zn(II)-Bound Metallo-Beta-Lactamse Vim-2 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 Structure of Zn(II)-Bound Metallo-Beta-Lactamse Vim-2 From Pseudomonas Aeruginosa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:20.7
occ:1.00
NE2 A:HIS114 2.2 12.9 1.0
NE2 A:HIS179 2.2 12.2 1.0
ND1 A:HIS116 2.2 18.8 1.0
O A:HOH659 2.2 31.4 1.0
O A:HOH601 2.6 32.1 1.0
CD2 A:HIS179 3.1 11.4 1.0
CE1 A:HIS114 3.1 11.6 1.0
CG A:HIS116 3.2 14.4 1.0
CE1 A:HIS116 3.2 15.6 1.0
CE1 A:HIS179 3.2 14.9 1.0
CD2 A:HIS114 3.2 16.1 1.0
CB A:HIS116 3.4 14.1 1.0
ZN A:ZN302 3.5 24.2 1.0
OD1 A:ASP118 3.7 19.9 1.0
O A:HOH609 4.1 23.7 1.0
SG A:CYS198 4.2 15.8 1.0
CB A:CYS198 4.2 13.7 1.0
ND1 A:HIS114 4.3 10.8 1.0
O A:HOH635 4.3 40.1 1.0
CG A:HIS179 4.3 7.8 1.0
ND1 A:HIS179 4.3 12.0 1.0
NE2 A:HIS116 4.3 16.2 1.0
CD2 A:HIS116 4.3 15.8 1.0
CG A:HIS114 4.3 10.7 1.0
OD2 A:ASP118 4.3 24.4 1.0
CG A:ASP118 4.5 24.3 1.0
O A:HOH666 4.7 47.3 1.0
CA A:HIS116 4.9 13.6 1.0

Zinc binding site 2 out of 3 in 4nq2

Go back to Zinc Binding Sites List in 4nq2
Zinc binding site 2 out of 3 in the Structure of Zn(II)-Bound Metallo-Beta-Lactamse Vim-2 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 Structure of Zn(II)-Bound Metallo-Beta-Lactamse Vim-2 From Pseudomonas Aeruginosa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn302

b:24.2
occ:1.00
SG A:CYS198 2.2 15.8 1.0
O A:HOH659 2.2 31.4 1.0
NE2 A:HIS240 2.3 23.5 1.0
OD2 A:ASP118 2.3 24.4 1.0
O A:HOH609 2.3 23.7 1.0
O A:HOH666 2.7 47.3 1.0
CE1 A:HIS240 3.2 20.5 1.0
CD2 A:HIS240 3.3 52.8 1.0
CG A:ASP118 3.3 24.3 1.0
CB A:CYS198 3.4 13.7 1.0
ZN A:ZN301 3.5 20.7 1.0
OD1 A:ASP118 3.7 19.9 1.0
NH2 A:ARG119 3.8 20.6 1.0
NE A:ARG119 4.2 14.3 1.0
O A:HOH601 4.2 32.1 1.0
O A:HOH445 4.2 26.3 1.0
NE2 A:HIS179 4.3 12.2 1.0
ND1 A:HIS240 4.3 19.5 1.0
CE1 A:HIS114 4.4 11.6 1.0
CG A:HIS240 4.4 16.4 1.0
CZ A:ARG119 4.4 18.3 1.0
CE1 A:HIS179 4.5 14.9 1.0
NE2 A:HIS114 4.5 12.9 1.0
CA A:CYS198 4.5 10.1 1.0
CB A:ASP118 4.6 23.6 1.0
O A:HOH667 4.8 57.0 1.0

Zinc binding site 3 out of 3 in 4nq2

Go back to Zinc Binding Sites List in 4nq2
Zinc binding site 3 out of 3 in the Structure of Zn(II)-Bound Metallo-Beta-Lactamse Vim-2 From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structure of Zn(II)-Bound Metallo-Beta-Lactamse Vim-2 From Pseudomonas Aeruginosa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn305

b:15.5
occ:1.00
NE2 A:HIS153 2.2 17.2 1.0
OXT A:ACT304 2.3 18.3 1.0
OXT A:ACT303 2.3 22.8 1.0
O A:ACT303 2.7 22.5 1.0
C A:ACT303 2.9 23.1 1.0
CE1 A:HIS153 3.0 20.4 1.0
C A:ACT304 3.2 17.6 1.0
O A:ACT304 3.3 16.8 1.0
CD2 A:HIS153 3.3 14.2 1.0
ND1 A:HIS153 4.2 15.4 1.0
CB A:ALA132 4.2 15.1 1.0
CH3 A:ACT303 4.3 23.9 1.0
CG A:HIS153 4.4 14.0 1.0
CH3 A:ACT304 4.6 18.0 1.0
CA A:ALA132 4.8 15.4 1.0
CG2 A:THR152 4.9 16.5 1.0
O A:HOH455 4.9 22.9 1.0

Reference:

M.Aitha, A.R.Marts, A.Bergstrom, A.J.Moller, L.Moritz, L.Turner, J.C.Nix, R.A.Bonomo, R.C.Page, D.L.Tierney, M.W.Crowder. Biochemical, Mechanistic, and Spectroscopic Characterization of Metallo-Beta-Lactamase Vim-2. Biochemistry 2014.
ISSN: ISSN 0006-2960
PubMed: 25356958
DOI: 10.1021/BI500916Y
Page generated: Wed Dec 16 05:37:27 2020

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