Zinc in PDB 1pe7: Thermolysin with Bicyclic Inhibitor

All present enzymatic activity of Thermolysin with Bicyclic Inhibitor:
3.4.24.27;

The structure of Thermolysin with Bicyclic Inhibitor, PDB code: 1pe7 was solved by D.Juers, N.Yusuff, P.A.Bartlett, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.82
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	93.800, 93.800, 131.400, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The structure of Thermolysin with Bicyclic Inhibitor also contains other interesting chemical elements:

Calcium

(Ca)

4 atoms

The binding sites of Zinc atom in the Thermolysin with Bicyclic Inhibitor (pdb code 1pe7). 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 Thermolysin with Bicyclic Inhibitor, PDB code: 1pe7:

Zinc binding site 1 out of 1 in the Thermolysin with Bicyclic Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Thermolysin with Bicyclic Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn317 b:14.5 occ:1.00 OP1 A:4BR322 2.0 10.3 1.0 NE2 A:HIS142 2.0 14.0 1.0 NE2 A:HIS146 2.0 10.9 1.0 OE2 A:GLU166 2.1 19.8 1.0 OE1 A:GLU166 2.6 25.2 1.0 CD A:GLU166 2.7 14.2 1.0 CE1 A:HIS146 2.9 11.2 1.0 P A:4BR322 2.9 13.9 1.0 OP2 A:4BR322 2.9 11.4 1.0 CD2 A:HIS142 3.0 9.9 1.0 CE1 A:HIS142 3.0 13.9 1.0 CD2 A:HIS146 3.1 16.8 1.0 OH A:TYR157 3.6 29.7 1.0 NE2 A:HIS231 3.9 13.7 1.0 CA A:LEU323 4.0 15.2 1.0 N A:LEU323 4.0 12.0 1.0 ND1 A:HIS146 4.1 13.9 1.0 CG A:GLU166 4.2 11.1 1.0 CG A:HIS142 4.2 14.0 1.0 ND1 A:HIS142 4.2 10.1 1.0 CG A:HIS146 4.2 9.1 1.0 CA2 A:4BR322 4.4 11.8 1.0 C A:LEU323 4.4 16.2 1.0 CD2 A:HIS231 4.6 18.6 1.0 CB A:SER169 4.6 7.0 1.0 O A:LEU323 4.6 14.8 1.0 CZ A:TYR157 4.7 40.6 1.0 OE1 A:GLU143 4.7 16.1 1.0 O A:HOH362 4.8 15.6 1.0 CA A:GLU166 4.8 12.5 1.0 OG A:SER169 4.9 9.7 1.0 CE1 A:HIS231 4.9 14.8 1.0 CE1 A:TYR157 4.9 0.0 1.0 CZ2 A:4BR322 5.0 17.4 1.0

P.A.Bartlett, N.Yusuff, M.K.Lindval, D.Holland, D.Juers, B.W.Matthews. Conformational Constraint and Structural Complementarity in Thermolysin Inhibitors: Structures of Enzyme Complexes and Conclusions To Be Published.