Zinc in PDB 5jss: Thermolysin in Complex with JC149.

All present enzymatic activity of Thermolysin in Complex with JC149.:
3.4.24.27;

The structure of Thermolysin in Complex with JC149., PDB code: 5jss 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)	40.07 / 1.19
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	92.528, 92.528, 131.314, 90.00, 90.00, 120.00
R / Rfree (%)	10.3 / 12.1

The structure of Thermolysin in Complex with JC149. also contains other interesting chemical elements:

Calcium

(Ca)

4 atoms

The binding sites of Zinc atom in the Thermolysin in Complex with JC149. (pdb code 5jss). 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 JC149., PDB code: 5jss:

Zinc binding site 1 out of 1 in the Thermolysin in Complex with JC149.


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 JC149. within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn401 b:5.8 occ:1.00 OE2 E:GLU166 2.0 6.0 1.0 O14 E:6NG406 2.0 5.6 1.0 NE2 E:HIS142 2.0 5.5 1.0 NE2 E:HIS146 2.0 5.4 1.0 CD E:GLU166 2.8 5.9 1.0 CE1 E:HIS146 2.9 5.9 1.0 OE1 E:GLU166 3.0 6.3 1.0 CE1 E:HIS142 3.0 5.6 1.0 P13 E:6NG406 3.0 5.7 1.0 HE1 E:HIS146 3.0 7.1 1.0 CD2 E:HIS142 3.0 5.3 1.0 O15 E:6NG406 3.1 6.3 1.0 CD2 E:HIS146 3.1 5.6 1.0 HH E:TYR157 3.1 8.8 1.0 HE1 E:HIS142 3.2 6.7 1.0 HD2 E:HIS142 3.2 6.4 1.0 HE2 E:HIS231 3.3 7.8 1.0 HD2 E:HIS146 3.4 6.7 1.0 OH E:TYR157 3.8 7.3 1.0 HA E:GLU166 4.0 6.9 1.0 NE2 E:HIS231 4.0 6.5 1.0 HB2 E:SER169 4.0 6.9 1.0 C17 E:6NG406 4.1 6.3 1.0 ND1 E:HIS146 4.1 5.9 1.0 N16 E:6NG406 4.1 6.5 1.0 ND1 E:HIS142 4.1 5.6 1.0 CG E:HIS142 4.2 5.5 1.0 CG E:HIS146 4.2 5.6 1.0 CG E:GLU166 4.2 5.9 1.0 HB3 E:SER169 4.2 6.9 1.0 HD2 E:HIS231 4.3 8.1 1.0 HE1 E:TYR157 4.4 8.3 1.0 HG2 E:GLU166 4.4 7.1 1.0 C12 E:6NG406 4.5 7.5 1.0 CB E:SER169 4.5 5.7 1.0 C22 E:6NG406 4.5 6.5 1.0 CD2 E:HIS231 4.5 6.8 1.0 N11 E:6NG406 4.6 9.2 0.3 C1 E:GOL407 4.6 10.1 1.0 O23 E:6NG406 4.6 6.6 1.0 OG E:SER169 4.7 6.2 1.0 O1 E:GOL407 4.7 7.4 1.0 HG3 E:GLU166 4.8 7.1 1.0 N11 E:6NG406 4.8 8.3 0.7 HH12 E:ARG203 4.8 7.8 1.0 CZ E:TYR157 4.8 6.8 1.0 HD1 E:HIS146 4.8 7.1 1.0 OE1 E:GLU143 4.8 9.7 1.0 CA E:GLU166 4.9 5.8 1.0 HD1 E:HIS142 4.9 6.8 1.0 CE1 E:TYR157 5.0 6.9 1.0

S.G.Krimmer, J.Cramer, M.Betz, V.Fridh, R.Karlsson, A.Heine, G.Klebe. Rational Design of Thermodynamic and Kinetic Binding Profiles By Optimizing Surface Water Networks Coating Protein-Bound Ligands. J. Med. Chem. V. 59 10530 2016.
ISSN: ISSN 1520-4804
PubMed: 27933956
DOI: 10.1021/ACS.JMEDCHEM.6B00998