Zinc in PDB 1pe8: Thermolysin with Monocyclic Inhibitor

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

The structure of Thermolysin with Monocyclic Inhibitor, PDB code: 1pe8 was solved by D.Juers, H.-J.Pyun, 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 / 1.80
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	93.700, 93.700, 131.600, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

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

Calcium

(Ca)

4 atoms

The binding sites of Zinc atom in the Thermolysin with Monocyclic Inhibitor (pdb code 1pe8). 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 Monocyclic Inhibitor, PDB code: 1pe8:

Zinc binding site 1 out of 1 in the Thermolysin with Monocyclic 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 Monocyclic Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn317 b:12.9 occ:1.00 NE2 A:HIS142 2.0 10.7 1.0 NE2 A:HIS146 2.0 8.8 1.0 OE2 A:GLU166 2.0 16.4 1.0 OP1 A:BR5322 2.0 11.9 1.0 CD A:GLU166 2.7 9.5 1.0 OE1 A:GLU166 2.8 19.3 1.0 CE1 A:HIS146 2.9 10.9 1.0 OP2 A:BR5322 2.9 13.2 1.0 P A:BR5322 3.0 13.8 1.0 CE1 A:HIS142 3.0 10.9 1.0 CD2 A:HIS142 3.0 8.5 1.0 CD2 A:HIS146 3.1 16.4 1.0 OH A:TYR157 3.7 23.0 1.0 NE2 A:HIS231 3.9 12.4 1.0 N A:LEU323 4.0 8.6 1.0 ND1 A:HIS146 4.1 11.7 1.0 CA A:LEU323 4.1 9.6 1.0 CG A:GLU166 4.1 9.0 1.0 ND1 A:HIS142 4.1 8.3 1.0 CG A:HIS142 4.1 11.0 1.0 CG A:HIS146 4.2 10.7 1.0 CA2 A:BR5322 4.4 14.2 1.0 CB A:SER169 4.5 6.6 1.0 C A:LEU323 4.6 19.6 1.0 CD2 A:HIS231 4.6 15.6 1.0 O A:LEU323 4.7 13.4 1.0 CZ A:TYR157 4.7 28.8 1.0 O A:HOH362 4.7 11.8 1.0 OE1 A:GLU143 4.7 13.8 1.0 OG A:SER169 4.8 8.8 1.0 CA A:GLU166 4.9 10.6 1.0 CE1 A:HIS231 4.9 11.8 1.0 CE1 A:TYR157 4.9 26.4 1.0 CZ2 A:BR5322 5.0 19.5 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.