Zinc in PDB 6d5o: Hexagonal Thermolysin (295 K) in the Presence of 50% Dmf

All present enzymatic activity of Hexagonal Thermolysin (295 K) in the Presence of 50% Dmf:
3.4.24.27;

The structure of Hexagonal Thermolysin (295 K) in the Presence of 50% Dmf, PDB code: 6d5o was solved by D.H.Juers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	13.97 / 2.00
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	93.931, 93.931, 131.656, 90.00, 90.00, 120.00
R / Rfree (%)	15.3 / 19.3

The structure of Hexagonal Thermolysin (295 K) in the Presence of 50% Dmf also contains other interesting chemical elements:

Calcium

(Ca)

4 atoms

The binding sites of Zinc atom in the Hexagonal Thermolysin (295 K) in the Presence of 50% Dmf (pdb code 6d5o). 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 Hexagonal Thermolysin (295 K) in the Presence of 50% Dmf, PDB code: 6d5o:

Zinc binding site 1 out of 1 in the Hexagonal Thermolysin (295 K) in the Presence of 50% Dmf


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Hexagonal Thermolysin (295 K) in the Presence of 50% Dmf within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn403 b:18.4 occ:1.00 O A:HOH508 1.9 20.3 0.9 OE2 A:GLU166 1.9 15.7 0.4 OE1 A:GLU166 2.0 12.1 0.6 NE2 A:HIS146 2.1 14.2 1.0 NE2 A:HIS142 2.1 16.3 1.0 CD A:GLU166 2.6 15.1 0.4 O A:HOH503 2.6 27.3 0.7 OE1 A:GLU166 2.8 14.0 0.4 CD A:GLU166 2.8 17.6 0.6 CE1 A:HIS146 3.0 13.6 1.0 OE2 A:GLU166 3.0 18.9 0.6 CE1 A:HIS142 3.0 16.8 1.0 CD2 A:HIS142 3.1 18.8 1.0 CD2 A:HIS146 3.1 11.8 1.0 O A:HOH501 3.1 17.3 0.8 HE1 A:HIS146 3.1 13.6 1.0 HE1 A:HIS142 3.2 16.8 1.0 HD2 A:HIS142 3.3 18.8 1.0 HD2 A:HIS146 3.3 11.8 1.0 HA A:VAL401 3.6 42.3 1.0 HA A:GLU166 3.9 14.4 0.4 HA A:GLU166 3.9 14.4 0.6 CG A:GLU166 4.0 13.1 0.4 HB2 A:SER169 4.1 16.8 1.0 ND1 A:HIS146 4.1 18.6 1.0 ND1 A:HIS142 4.2 14.8 1.0 HG2 A:GLU166 4.2 13.6 0.4 CG A:HIS142 4.2 13.2 1.0 CG A:HIS146 4.2 13.8 1.0 NE2 A:HIS231 4.2 17.8 1.0 O A:HOH608 4.3 31.6 1.0 CG A:GLU166 4.3 13.6 0.6 OH A:TYR157 4.3 31.8 0.5 HE2 A:TYR157 4.3 14.7 0.5 HB3 A:SER169 4.4 16.8 1.0 CA A:VAL401 4.4 42.3 1.0 OE1 A:GLU143 4.5 20.2 1.0 HD2 A:HIS231 4.5 23.7 1.0 HB3 A:GLU166 4.5 17.3 0.6 CB A:SER169 4.6 16.8 1.0 HG3 A:GLU166 4.6 13.6 0.4 HH22 A:ARG203 4.7 16.9 1.0 C A:VAL401 4.7 40.5 1.0 CA A:GLU166 4.7 14.4 0.6 CD2 A:HIS231 4.7 23.7 1.0 OG A:SER169 4.7 18.5 1.0 CA A:GLU166 4.8 14.4 0.4 CB A:GLU166 4.8 17.3 0.6 HG3 A:GLU166 4.8 13.6 0.6 O A:VAL401 4.8 26.2 1.0 HG2 A:GLU166 4.8 13.6 0.6 N A:VAL401 4.8 32.2 1.0 HH A:TYR157 4.8 43.9 0.5 CB A:GLU166 4.8 17.3 0.4 OE2 A:GLU143 4.9 26.3 1.0 HD1 A:HIS146 4.9 18.6 1.0 HD1 A:HIS142 4.9 14.8 1.0 HB3 A:GLU166 4.9 17.3 0.4 HG23 A:VAL401 5.0 28.7 1.0 CD A:GLU143 5.0 22.3 1.0

D.H.Juers, C.A.Farley, C.P.Saxby, R.A.Cotter, J.K.B.Cahn, R.C.Holton-Burke, K.Harrison, Z.Wu. The Impact of Cryosolution Thermal Contraction on Proteins and Protein Crystals: Volumes, Conformation and Order. Acta Crystallogr D Struct V. 74 922 2018BIOL.
ISSN: ISSN 2059-7983
PubMed: 30198901
DOI: 10.1107/S2059798318008793