Zinc in PDB 2whz: Dipeptide Inhibitors of Thermolysin

All present enzymatic activity of Dipeptide Inhibitors of Thermolysin:
3.4.24.27;

The structure of Dipeptide Inhibitors of Thermolysin, PDB code: 2whz was solved by B.A.Lund, I.Leiros, H.-K.S.Leiros, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.75
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	92.890, 92.890, 127.740, 90.00, 90.00, 120.00
R / Rfree (%)	15.9 / 19.7

The structure of Dipeptide Inhibitors of Thermolysin also contains other interesting chemical elements:

Calcium

(Ca)

4 atoms

The binding sites of Zinc atom in the Dipeptide Inhibitors of Thermolysin (pdb code 2whz). 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 Dipeptide Inhibitors of Thermolysin, PDB code: 2whz:

Zinc binding site 1 out of 1 in the Dipeptide Inhibitors of Thermolysin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Dipeptide Inhibitors of Thermolysin within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1317 b:15.3 occ:1.00 NE2 A:HIS142 2.0 14.5 1.0 OE2 A:GLU166 2.0 12.1 1.0 NE2 A:HIS146 2.1 11.5 1.0 O A:HOH2351 2.3 10.5 1.0 CD A:GLU166 2.8 15.8 1.0 CD2 A:HIS142 3.0 9.5 1.0 OE1 A:GLU166 3.0 14.7 1.0 CE1 A:HIS142 3.0 14.1 1.0 CE1 A:HIS146 3.0 15.4 1.0 CD2 A:HIS146 3.1 12.8 1.0 OH A:TYR157 3.8 21.1 1.0 ND1 A:HIS142 4.1 11.2 1.0 CG A:HIS142 4.1 9.5 1.0 ND1 A:HIS146 4.2 12.0 1.0 NE2 A:HIS231 4.2 15.3 1.0 CG A:HIS146 4.2 14.0 1.0 CG A:GLU166 4.2 11.0 1.0 OE1 A:GLU143 4.3 16.5 1.0 O A:HOH2190 4.4 17.3 1.0 CB A:SER169 4.5 12.0 1.0 CA A:ILE1001 4.5 17.8 1.0 N A:ILE1001 4.6 16.8 1.0 CD2 A:HIS231 4.6 17.3 1.0 O A:ILE1001 4.7 17.0 1.0 OG A:SER169 4.7 11.9 1.0 C A:ILE1001 4.8 18.4 1.0 CZ A:TYR157 4.8 20.9 1.0 CE1 A:TYR157 4.9 18.9 1.0 CA A:GLU166 4.9 10.6 1.0

B.A.Lund, I.Leiros, H.-K.S.Leiros. Dipeptide Inhibitors of Thermolysin To Be Published.