Zinc in PDB 5m69: Thermolysin in Complex with Inhibitor and Xenon

All present enzymatic activity of Thermolysin in Complex with Inhibitor and Xenon:
3.4.24.27;

The structure of Thermolysin in Complex with Inhibitor and Xenon, PDB code: 5m69 was solved by S.G.Krimmer, J.Cramer, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.24 / 1.44
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	92.476, 92.476, 129.938, 90.00, 90.00, 120.00
R / Rfree (%)	10.8 / 14.1

The structure of Thermolysin in Complex with Inhibitor and Xenon also contains other interesting chemical elements:

Xenon	(Xe)	2 atoms
Calcium	(Ca)	4 atoms

The binding sites of Zinc atom in the Thermolysin in Complex with Inhibitor and Xenon (pdb code 5m69). 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 in Complex with Inhibitor and Xenon, PDB code: 5m69:

Zinc binding site 1 out of 1 in the Thermolysin in Complex with Inhibitor and Xenon


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Thermolysin in Complex with Inhibitor and Xenon within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn401 b:11.0 occ:1.00 O30 E:7GR408 2.0 10.6 1.0 OE2 E:GLU166 2.0 10.6 1.0 NE2 E:HIS142 2.0 9.1 1.0 NE2 E:HIS146 2.0 9.2 1.0 CD E:GLU166 2.8 10.4 1.0 CE1 E:HIS146 2.9 9.2 1.0 OE1 E:GLU166 3.0 10.8 1.0 CE1 E:HIS142 3.0 9.1 1.0 CD2 E:HIS142 3.0 9.8 1.0 HE1 E:HIS146 3.0 11.0 1.0 P28 E:7GR408 3.0 12.1 1.0 HH E:TYR157 3.1 15.5 1.0 O29 E:7GR408 3.1 13.2 1.0 CD2 E:HIS146 3.1 9.6 1.0 HE1 E:HIS142 3.2 10.9 1.0 HD2 E:HIS142 3.2 11.7 1.0 HE2 E:HIS231 3.3 13.4 1.0 HD2 E:HIS146 3.4 11.5 1.0 OH E:TYR157 3.8 12.9 1.0 HA E:GLU166 4.0 10.5 1.0 NE2 E:HIS231 4.0 11.2 1.0 ND1 E:HIS146 4.1 9.5 1.0 N1 E:7GR408 4.1 12.1 1.0 HB2 E:SER169 4.1 10.3 1.0 ND1 E:HIS142 4.1 9.2 1.0 C2 E:7GR408 4.1 12.7 1.0 CG E:HIS142 4.1 9.7 1.0 CG E:GLU166 4.2 10.1 1.0 CG E:HIS146 4.2 8.9 1.0 HB3 E:SER169 4.2 10.3 1.0 HE1 E:TYR157 4.3 14.2 1.0 HD2 E:HIS231 4.4 13.0 1.0 HG2 E:GLU166 4.4 12.1 1.0 C31 E:7GR408 4.5 16.0 1.0 CB E:SER169 4.5 8.6 1.0 N34 E:7GR408 4.5 19.0 0.5 CD2 E:HIS231 4.5 10.8 1.0 C1 E:GOL407 4.6 19.5 1.0 C5 E:7GR408 4.6 14.0 1.0 OG E:SER169 4.7 10.2 1.0 OE1 E:GLU143 4.7 14.5 1.0 HG3 E:GLU166 4.7 12.1 1.0 CZ E:TYR157 4.8 12.4 1.0 O1 E:GOL407 4.8 13.3 1.0 N34 E:7GR408 4.8 18.6 0.5 HD1 E:HIS146 4.8 11.4 1.0 O6 E:7GR408 4.8 14.9 1.0 CA E:GLU166 4.9 8.7 1.0 CE1 E:TYR157 4.9 11.8 1.0 HD1 E:HIS142 4.9 11.0 1.0 HH12 E:ARG203 4.9 12.7 1.0

S.G.Krimmer, J.Cramer, J.Schiebel, A.Heine, G.Klebe. How Nothing Boosts Affinity: Hydrophobic Ligand Binding to the Virtually Vacated S1' Pocket of Thermolysin. J. Am. Chem. Soc. V. 139 10419 2017.
ISSN: ESSN 1520-5126
PubMed: 28696673
DOI: 10.1021/JACS.7B05028