Zinc in PDB 6fsm: Crystal Structure of Tce-Treated Thermolysin

All present enzymatic activity of Crystal Structure of Tce-Treated Thermolysin:
3.4.24.27;

The structure of Crystal Structure of Tce-Treated Thermolysin, PDB code: 6fsm was solved by C.Pichlo, U.Baumann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.47 / 1.39
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	92.948, 92.948, 129.668, 90.00, 90.00, 120.00
R / Rfree (%)	14.8 / 16.2

The structure of Crystal Structure of Tce-Treated Thermolysin also contains other interesting chemical elements:

Calcium

(Ca)

4 atoms

The binding sites of Zinc atom in the Crystal Structure of Tce-Treated Thermolysin (pdb code 6fsm). 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 Crystal Structure of Tce-Treated Thermolysin, PDB code: 6fsm:

Zinc binding site 1 out of 1 in the Crystal Structure of Tce-Treated Thermolysin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Tce-Treated Thermolysin within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:12.7 occ:1.00 OE2 A:GLU166 2.0 14.9 1.0 O4 A:PO4406 2.0 23.8 0.9 NE2 A:HIS142 2.0 10.9 1.0 NE2 A:HIS146 2.0 12.9 1.0 O2 A:PO4406 2.8 37.5 0.9 CD A:GLU166 2.8 12.8 1.0 P A:PO4406 2.8 31.7 0.9 CE1 A:HIS146 2.9 12.7 1.0 CD2 A:HIS142 3.0 11.0 1.0 OE1 A:GLU166 3.0 12.2 1.0 CE1 A:HIS142 3.0 11.0 1.0 HE1 A:HIS146 3.1 15.3 1.0 CD2 A:HIS146 3.1 11.4 1.0 HD2 A:HIS142 3.1 13.2 1.0 HH A:TYR157 3.2 18.3 1.0 HE1 A:HIS142 3.2 13.2 1.0 HD2 A:HIS146 3.3 13.7 1.0 HE2 A:HIS231 3.5 16.7 1.0 O1 A:PO4406 3.5 35.0 0.9 HA A:VAL410 3.8 29.8 0.9 OH A:TYR157 3.9 15.2 1.0 HA A:GLU166 3.9 14.5 1.0 HB2 A:SER169 4.0 12.7 1.0 ND1 A:HIS146 4.1 12.8 1.0 ND1 A:HIS142 4.1 11.8 1.0 CG A:HIS142 4.1 11.1 1.0 NE2 A:HIS231 4.2 13.9 1.0 O3 A:PO4406 4.2 33.4 0.9 CG A:HIS146 4.2 12.7 1.0 HB3 A:SER169 4.2 12.7 1.0 CG A:GLU166 4.2 11.6 1.0 HE1 A:TYR157 4.3 18.5 1.0 HG2 A:GLU166 4.4 13.9 1.0 OE1 A:GLU143 4.4 14.9 0.8 CB A:SER169 4.5 10.6 1.0 OE2 A:GLU143 4.6 17.9 0.2 HD2 A:HIS231 4.6 16.7 1.0 O A:HOH516 4.6 19.0 1.0 OG A:SER169 4.7 12.5 1.0 CA A:VAL410 4.7 24.9 0.9 CD2 A:HIS231 4.7 13.9 1.0 OE1 A:GLU143 4.7 18.2 0.2 HG3 A:GLU166 4.8 13.9 1.0 CA A:GLU166 4.8 12.1 1.0 HD1 A:HIS146 4.8 15.4 1.0 CZ A:TYR157 4.8 14.5 1.0 HD1 A:HIS142 4.9 14.2 1.0 HH22 A:ARG203 4.9 15.2 1.0 O A:VAL410 4.9 23.8 0.9 H12 A:GOL407 4.9 57.0 1.0 CE1 A:TYR157 4.9 15.4 1.0 CD A:GLU143 5.0 13.2 0.2 C A:VAL410 5.0 32.1 0.9

C.Pichlo, C.Toelzer, K.Chojnacki, S.Ocal, M.Uthoff, S.Ruegenberg, T.Hermanns, M.Schacherl, M.S.Denzel, K.Hofmann, K.Niefind, U.Baumann. Improved Protein-Crystal Identification By Using 2,2,2-Trichloroethanol As A Fluorescence Enhancer. Acta Crystallogr F Struct V. 74 307 2018BIOL Commun.
ISSN: ESSN 2053-230X
PubMed: 29717999
DOI: 10.1107/S2053230X18005253