Zinc in PDB 1kei: Thermolysin (Substrate-Free)

All present enzymatic activity of Thermolysin (Substrate-Free):
3.4.24.27;

The structure of Thermolysin (Substrate-Free), PDB code: 1kei was solved by M.Senda, T.Senda, S.Kidokoro, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.48 / 1.60
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	93.541, 93.541, 131.141, 90.00, 90.00, 120.00
R / Rfree (%)	17.2 / 18.8

The structure of Thermolysin (Substrate-Free) also contains other interesting chemical elements:

Calcium

(Ca)

4 atoms

The binding sites of Zinc atom in the Thermolysin (Substrate-Free) (pdb code 1kei). 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 (Substrate-Free), PDB code: 1kei:

Zinc binding site 1 out of 1 in the Thermolysin (Substrate-Free)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Thermolysin (Substrate-Free) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn405 b:14.3 occ:1.00 OE2 A:GLU166 1.8 20.4 1.0 NE2 A:HIS146 2.0 11.5 1.0 NE2 A:HIS142 2.1 14.1 1.0 CD A:GLU166 2.7 19.6 1.0 CE1 A:HIS146 2.9 14.4 1.0 OE1 A:GLU166 3.0 23.6 1.0 CE1 A:HIS142 3.0 14.2 1.0 CD2 A:HIS146 3.0 14.5 1.0 CD2 A:HIS142 3.0 12.9 1.0 OH A:TYR157 3.9 23.1 0.5 ND1 A:HIS146 4.1 13.5 1.0 CG A:GLU166 4.1 15.7 1.0 ND1 A:HIS142 4.1 11.7 1.0 CG A:HIS146 4.2 12.5 1.0 CG A:HIS142 4.2 12.7 1.0 NE2 A:HIS231 4.3 19.0 1.0 OE1 A:GLU143 4.5 19.8 1.0 O A:HOH1137 4.5 25.2 1.0 CB A:SER169 4.5 11.4 1.0 CA A:VAL1001 4.5 31.2 1.0 OG A:SER169 4.6 13.0 1.0 OE2 A:GLU143 4.7 25.7 1.0 CA A:GLU166 4.7 13.0 1.0 N A:VAL1001 4.8 30.2 1.0 CD2 A:HIS231 4.8 19.5 1.0 O A:HOH1185 4.8 36.8 1.0 C A:VAL1001 4.8 31.7 1.0 O A:VAL1001 4.9 31.3 1.0 CZ A:TYR157 4.9 21.9 0.5 CE1 A:TYR157 4.9 21.8 0.5 CD A:GLU143 4.9 19.1 1.0 CB A:GLU166 4.9 14.1 1.0

M.Senda, T.Senda, S.Kidokoro. Crystal Structure Analyses of Thermolysin in Complex with Its Inhibitors To Be Published.