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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

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: Sat Sep 26 02:07:42 2020
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