Atomistry » Zinc » PDB 3ttf-3u6e » 3tzb
Atomistry »
  Zinc »
    PDB 3ttf-3u6e »
      3tzb »

Zinc in PDB 3tzb: Quinone Oxidoreductase (NQ02) Bound to NSC13000

Enzymatic activity of Quinone Oxidoreductase (NQ02) Bound to NSC13000

All present enzymatic activity of Quinone Oxidoreductase (NQ02) Bound to NSC13000:
1.10.99.2;

Protein crystallography data

The structure of Quinone Oxidoreductase (NQ02) Bound to NSC13000, PDB code: 3tzb was solved by M.S.Dunstan, D.Leys, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.20 / 2.19
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 50.620, 62.101, 78.506, 92.95, 90.10, 110.45
R / Rfree (%) 16.7 / 23.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Quinone Oxidoreductase (NQ02) Bound to NSC13000 (pdb code 3tzb). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Quinone Oxidoreductase (NQ02) Bound to NSC13000, PDB code: 3tzb:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 3tzb

Go back to Zinc Binding Sites List in 3tzb
Zinc binding site 1 out of 4 in the Quinone Oxidoreductase (NQ02) Bound to NSC13000


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Quinone Oxidoreductase (NQ02) Bound to NSC13000 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn231

b:35.6
occ:1.00
ND1 A:HIS173 2.1 19.7 1.0
ND1 A:HIS177 2.2 33.3 1.0
SG A:CYS222 2.7 51.5 1.0
CB A:CYS222 2.9 87.4 1.0
CE1 A:HIS173 3.0 22.0 1.0
O A:CYS222 3.0 57.5 1.0
CE1 A:HIS177 3.1 30.9 1.0
CG A:HIS177 3.1 38.6 1.0
CG A:HIS173 3.1 16.6 1.0
C A:CYS222 3.3 74.1 1.0
CB A:HIS177 3.4 22.0 1.0
CB A:HIS173 3.5 16.0 1.0
CA A:CYS222 3.6 82.1 1.0
CA A:HIS173 3.8 15.3 1.0
NE2 A:HIS177 4.1 37.3 1.0
N A:THR223 4.1 82.4 1.0
CD2 A:HIS177 4.1 47.1 1.0
NE2 A:HIS173 4.1 29.1 1.0
CD2 A:HIS173 4.2 19.2 1.0
O A:HIS173 4.6 15.7 1.0
C A:HIS173 4.7 13.4 1.0
CA A:THR223 4.8 90.1 1.0
N A:HIS173 4.9 19.4 1.0
CE1 A:TYR132 4.9 15.7 1.0
CD1 A:TYR132 4.9 17.0 1.0
N A:CYS222 4.9 70.2 1.0
CA A:HIS177 5.0 17.1 1.0

Zinc binding site 2 out of 4 in 3tzb

Go back to Zinc Binding Sites List in 3tzb
Zinc binding site 2 out of 4 in the Quinone Oxidoreductase (NQ02) Bound to NSC13000


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Quinone Oxidoreductase (NQ02) Bound to NSC13000 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn231

b:39.7
occ:1.00
ND1 B:HIS177 2.2 30.4 1.0
ND1 B:HIS173 2.2 29.0 1.0
O B:CYS222 2.6 0.8 1.0
SG B:CYS222 2.8 66.4 1.0
CB B:CYS222 2.9 0.8 1.0
C B:CYS222 3.1 0.4 1.0
CG B:HIS177 3.1 28.1 1.0
CE1 B:HIS173 3.1 32.5 1.0
CE1 B:HIS177 3.2 34.5 1.0
CG B:HIS173 3.3 26.0 1.0
CB B:HIS177 3.4 16.3 1.0
CA B:CYS222 3.6 0.3 1.0
CB B:HIS173 3.6 7.9 1.0
CA B:HIS173 3.8 19.5 1.0
N B:THR223 3.9 0.7 1.0
NE2 B:HIS177 4.2 39.5 1.0
CD2 B:HIS177 4.2 30.8 1.0
NE2 B:HIS173 4.3 32.5 1.0
CD2 B:HIS173 4.4 32.2 1.0
CA B:THR223 4.4 0.7 1.0
N B:CYS222 4.8 94.0 1.0
C B:HIS173 4.8 19.3 1.0
O B:HIS173 4.8 23.0 1.0
N B:HIS173 4.8 22.1 1.0
CA B:HIS177 4.9 14.6 1.0
O B:GLN172 5.0 25.0 1.0

Zinc binding site 3 out of 4 in 3tzb

Go back to Zinc Binding Sites List in 3tzb
Zinc binding site 3 out of 4 in the Quinone Oxidoreductase (NQ02) Bound to NSC13000


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Quinone Oxidoreductase (NQ02) Bound to NSC13000 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn231

b:32.2
occ:1.00
ND1 C:HIS173 2.1 19.6 1.0
ND1 C:HIS177 2.4 27.8 1.0
SG C:CYS222 2.5 51.2 1.0
CB C:CYS222 2.8 83.6 1.0
O C:CYS222 2.8 67.8 1.0
CE1 C:HIS173 3.1 20.5 1.0
CG C:HIS173 3.2 19.2 1.0
C C:CYS222 3.3 80.4 1.0
CG C:HIS177 3.3 25.3 1.0
CE1 C:HIS177 3.3 24.0 1.0
CB C:HIS177 3.5 16.5 1.0
CA C:CYS222 3.5 79.4 1.0
CB C:HIS173 3.6 15.6 1.0
CA C:HIS173 3.9 15.5 1.0
NE2 C:HIS173 4.2 26.4 1.0
N C:THR223 4.2 89.1 1.0
CD2 C:HIS173 4.3 17.7 1.0
NE2 C:HIS177 4.4 27.6 1.0
CD2 C:HIS177 4.4 27.0 1.0
O C:HIS173 4.7 22.8 1.0
C C:HIS173 4.7 13.5 1.0
CA C:THR223 4.8 0.3 1.0
N C:CYS222 4.8 61.0 1.0
N C:HIS173 4.9 18.4 1.0
CD1 C:TYR132 5.0 22.6 1.0

Zinc binding site 4 out of 4 in 3tzb

Go back to Zinc Binding Sites List in 3tzb
Zinc binding site 4 out of 4 in the Quinone Oxidoreductase (NQ02) Bound to NSC13000


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Quinone Oxidoreductase (NQ02) Bound to NSC13000 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn231

b:30.4
occ:1.00
ND1 D:HIS173 2.3 23.1 1.0
ND1 D:HIS177 2.3 28.6 1.0
O D:CYS222 2.6 34.6 1.0
CB D:CYS222 2.7 77.6 1.0
SG D:CYS222 2.7 55.6 1.0
C D:CYS222 3.1 63.5 1.0
CG D:HIS177 3.2 26.9 1.0
CE1 D:HIS173 3.2 19.1 1.0
CE1 D:HIS177 3.2 24.0 1.0
CG D:HIS173 3.2 25.8 1.0
CA D:CYS222 3.4 71.8 1.0
CB D:HIS177 3.5 16.5 1.0
CB D:HIS173 3.5 14.2 1.0
CA D:HIS173 3.7 14.4 1.0
N D:THR223 4.1 79.6 1.0
NE2 D:HIS177 4.3 27.2 1.0
CD2 D:HIS177 4.3 27.9 1.0
NE2 D:HIS173 4.3 28.3 1.0
CD2 D:HIS173 4.4 27.7 1.0
C D:HIS173 4.7 9.7 1.0
N D:HIS173 4.7 12.4 1.0
N D:CYS222 4.7 63.7 1.0
CA D:THR223 4.8 93.2 1.0
O D:HIS173 4.8 21.0 1.0
O D:GLN172 5.0 24.4 1.0

Reference:

K.A.Nolan, M.S.Dunstan, M.C.Caraher, K.A.Scott, D.Leys, I.J.Stratford. In Silico Screening Reveals Structurally Diverse, Nanomolar Inhibitors of NQO2 That Are Functionally Active in Cells and Can Modulate Nf-Kappa B Signaling. Mol.Cancer Ther. V. 11 194 2012.
ISSN: ISSN 1535-7163
PubMed: 22090421
DOI: 10.1158/1535-7163.MCT-11-0543
Page generated: Wed Dec 16 04:53:12 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy