Atomistry » Zinc » PDB 2geh-2gzg » 2geh
Atomistry »
  Zinc »
    PDB 2geh-2gzg »
      2geh »

Zinc in PDB 2geh: N-Hydroxyurea, A Versatile Zinc Binding Function in the Design of Metalloenzyme Inhibitors

Enzymatic activity of N-Hydroxyurea, A Versatile Zinc Binding Function in the Design of Metalloenzyme Inhibitors

All present enzymatic activity of N-Hydroxyurea, A Versatile Zinc Binding Function in the Design of Metalloenzyme Inhibitors:
4.2.1.1;

Protein crystallography data

The structure of N-Hydroxyurea, A Versatile Zinc Binding Function in the Design of Metalloenzyme Inhibitors, PDB code: 2geh was solved by C.Temperini, A.Innocenti, A.Scozzafava, C.T.Supuran, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.201, 41.453, 72.268, 90.00, 104.40, 90.00
R / Rfree (%) 19.9 / 22.9

Other elements in 2geh:

The structure of N-Hydroxyurea, A Versatile Zinc Binding Function in the Design of Metalloenzyme Inhibitors also contains other interesting chemical elements:

Mercury (Hg) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the N-Hydroxyurea, A Versatile Zinc Binding Function in the Design of Metalloenzyme Inhibitors (pdb code 2geh). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the N-Hydroxyurea, A Versatile Zinc Binding Function in the Design of Metalloenzyme Inhibitors, PDB code: 2geh:

Zinc binding site 1 out of 1 in 2geh

Go back to Zinc Binding Sites List in 2geh
Zinc binding site 1 out of 1 in the N-Hydroxyurea, A Versatile Zinc Binding Function in the Design of Metalloenzyme Inhibitors


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of N-Hydroxyurea, A Versatile Zinc Binding Function in the Design of Metalloenzyme Inhibitors within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:8.8
occ:1.00
 O1 A:NHY300 1.9 29.0 1.0
N1 A:NHY300 2.0 29.1 1.0
NE2 A:HIS96 2.0 4.5 1.0
ND1 A:HIS119 2.1 2.0 1.0
NE2 A:HIS94 2.1 3.5 1.0
CE1 A:HIS119 2.9 2.0 1.0
CD2 A:HIS96 2.9 3.3 1.0
CD2 A:HIS94 2.9 3.9 1.0
CE1 A:HIS96 3.1 5.3 1.0
CE1 A:HIS94 3.1 3.4 1.0
CG A:HIS119 3.1 2.0 1.0
C A:NHY300 3.2 30.0 1.0
CB A:HIS119 3.6 2.0 1.0
OG1 A:THR199 3.7 3.7 1.0
O A:HOH382 3.8 11.1 1.0
N2 A:NHY300 4.0 30.7 1.0
OE1 A:GLU106 4.0 3.1 1.0
O2 A:NHY300 4.0 30.5 1.0
NE2 A:HIS119 4.1 2.0 1.0
CG A:HIS96 4.1 2.4 1.0
CG A:HIS94 4.1 3.1 1.0
ND1 A:HIS96 4.2 2.4 1.0
ND1 A:HIS94 4.2 4.0 1.0
CD2 A:HIS119 4.2 2.0 1.0
O A:HOH399 4.6 11.2 1.0
CD A:GLU106 4.9 3.2 1.0

Reference:

C.Temperini, A.Innocenti, A.Scozzafava, C.T.Supuran. N-Hydroxyurea-A Versatile Zinc Binding Function in the Design of Metalloenzyme Inhibitors. Bioorg.Med.Chem.Lett. V. 16 4316 2006.
ISSN: ISSN 0960-894X
PubMed: 16759856
DOI: 10.1016/J.BMCL.2006.05.068
Page generated: Thu Oct 17 00:17:42 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