Zinc in PDB 3flf: Thermolysin Inhibition

All present enzymatic activity of Thermolysin Inhibition:
3.4.24.27;

The structure of Thermolysin Inhibition, PDB code: 3flf was solved by L.Englert, A.Biela, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.97
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	92.658, 92.658, 130.477, 90.00, 90.00, 120.00
R / Rfree (%)	20 / 26.5

The structure of Thermolysin Inhibition also contains other interesting chemical elements:

Calcium

(Ca)

4 atoms

The binding sites of Zinc atom in the Thermolysin Inhibition (pdb code 3flf). 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 Inhibition, PDB code: 3flf:

Zinc binding site 1 out of 1 in the Thermolysin Inhibition


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Thermolysin Inhibition within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2004 b:15.4 occ:1.00 OE2 A:GLU166 1.9 15.3 1.0 O11 A:UB33000 2.0 16.6 1.0 NE2 A:HIS146 2.1 13.4 1.0 NE2 A:HIS142 2.1 9.5 1.0 CD A:GLU166 2.7 16.1 1.0 OE1 A:GLU166 2.8 16.1 1.0 CD2 A:HIS142 2.9 8.8 1.0 CE1 A:HIS146 3.0 11.9 1.0 P10 A:UB33000 3.0 17.6 1.0 CD2 A:HIS146 3.1 8.5 1.0 O12 A:UB33000 3.1 16.1 1.0 CE1 A:HIS142 3.1 11.8 1.0 OH A:TYR157 3.9 19.4 1.0 C14 A:UB33000 3.9 19.7 1.0 NE2 A:HIS231 4.0 15.6 1.0 N13 A:UB33000 4.0 14.6 1.0 CG A:HIS142 4.1 12.4 1.0 ND1 A:HIS146 4.1 10.3 1.0 CG A:GLU166 4.1 11.9 1.0 ND1 A:HIS142 4.2 13.3 1.0 CG A:HIS146 4.2 12.2 1.0 C9 A:UB33000 4.5 17.8 1.0 C3 A:GOL5000 4.5 20.8 1.0 CB A:SER169 4.6 8.6 1.0 CD2 A:HIS231 4.6 14.9 1.0 N8 A:UB33000 4.6 23.8 1.0 C18 A:UB33000 4.6 19.3 1.0 OG A:SER169 4.7 15.7 1.0 O3 A:GOL5000 4.8 16.2 1.0 O28 A:UB33000 4.9 17.2 1.0 CA A:GLU166 4.9 15.7 1.0 CZ A:TYR157 4.9 19.6 1.0 OE1 A:GLU143 5.0 16.2 1.0 CE1 A:HIS231 5.0 14.9 1.0

L.Englert, A.Biela, M.Zayed, A.Heine, D.Hangauer, G.Klebe. Displacement of Disordered Water Molecules From Hydrophobic Pocket Creates Enthalpic Signature: Binding of Phosphonamidate to the S1'-Pocket of Thermolysin. Biochim.Biophys.Acta V.1800 1192 2010.
ISSN: ISSN 0006-3002
PubMed: 20600625
DOI: 10.1016/J.BBAGEN.2010.06.009