Zinc in PDB 1pe5: Thermolysin with Tricyclic Inhibitor

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

The structure of Thermolysin with Tricyclic Inhibitor, PDB code: 1pe5 was solved by D.Juers, D.Holland, B.P.Morgan, 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 / 1.70
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 Tricyclic Inhibitor also contains other interesting chemical elements:

Calcium

(Ca)

4 atoms

The binding sites of Zinc atom in the Thermolysin with Tricyclic Inhibitor (pdb code 1pe5). 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 Tricyclic Inhibitor, PDB code: 1pe5:

Zinc binding site 1 out of 1 in the Thermolysin with Tricyclic 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 Tricyclic Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn317 b:10.2 occ:1.00 OP1 A:BR3322 1.9 7.9 1.0 NE2 A:HIS146 2.0 4.6 1.0 NE2 A:HIS142 2.0 8.8 1.0 OE1 A:GLU166 2.1 19.4 1.0 OE2 A:GLU166 2.5 23.3 1.0 CD A:GLU166 2.6 12.2 1.0 CE1 A:HIS146 2.9 7.1 1.0 P A:BR3322 2.9 8.8 1.0 CE1 A:HIS142 3.0 8.7 1.0 OP2 A:BR3322 3.0 8.1 1.0 CD2 A:HIS142 3.1 10.8 1.0 CD2 A:HIS146 3.1 9.2 1.0 OH A:TYR157 3.8 23.3 1.0 NE2 A:HIS231 3.9 8.1 1.0 N A:LEU323 4.0 5.8 1.0 CA A:LEU323 4.0 7.0 1.0 ND1 A:HIS146 4.1 7.2 1.0 CG A:GLU166 4.2 5.6 1.0 CG A:HIS146 4.2 7.2 1.0 ND1 A:HIS142 4.2 6.7 1.0 CG A:HIS142 4.2 7.0 1.0 CA2 A:BR3322 4.4 8.8 1.0 C A:LEU323 4.5 13.3 1.0 CD2 A:HIS231 4.5 15.7 1.0 CB A:SER169 4.6 6.3 1.0 O A:LEU323 4.7 11.9 1.0 OG A:SER169 4.8 6.6 1.0 O A:HOH549 4.8 11.3 1.0 CA A:GLU166 4.8 7.3 1.0 CZ A:TYR157 4.8 0.0 1.0 OE1 A:GLU143 4.9 13.7 1.0 CB A:GLU166 4.9 6.7 1.0 CZ2 A:BR3322 5.0 11.2 1.0 CE1 A:HIS231 5.0 13.1 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.