Zinc in PDB 1fjw: Thermolysin (50 Mm Phenol Soaked)

All present enzymatic activity of Thermolysin (50 Mm Phenol Soaked):
3.4.24.27;

The structure of Thermolysin (50 Mm Phenol Soaked), PDB code: 1fjw was solved by A.C.English, C.R.Groom, R.E.Hubbard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 1.90
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	93.960, 93.960, 130.915, 90.00, 90.00, 120.00
R / Rfree (%)	16.3 / 19.4

The structure of Thermolysin (50 Mm Phenol Soaked) also contains other interesting chemical elements:

Calcium

(Ca)

4 atoms

The binding sites of Zinc atom in the Thermolysin (50 Mm Phenol Soaked) (pdb code 1fjw). 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 (50 Mm Phenol Soaked), PDB code: 1fjw:

Zinc binding site 1 out of 1 in the Thermolysin (50 Mm Phenol Soaked)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Thermolysin (50 Mm Phenol Soaked) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:24.3 occ:1.00 NE2 A:HIS146 2.0 18.5 1.0 NE2 A:HIS142 2.0 22.6 1.0 OE1 A:GLU166 2.2 30.6 1.0 OE2 A:GLU166 2.3 32.5 1.0 O A:HOH510 2.5 38.4 1.0 CD A:GLU166 2.8 29.5 1.0 CE1 A:HIS146 3.0 23.0 1.0 CE1 A:HIS142 3.0 20.1 1.0 CD2 A:HIS142 3.0 23.8 1.0 CD2 A:HIS146 3.1 19.8 1.0 OE2 A:GLU143 3.8 25.4 1.0 OH A:TYR157 3.9 25.3 0.4 ND1 A:HIS146 4.1 20.9 1.0 CG A:HIS146 4.1 18.8 1.0 ND1 A:HIS142 4.2 20.7 1.0 CG A:HIS142 4.2 20.3 1.0 CG A:GLU166 4.3 18.7 1.0 O1 A:IPH507 4.3 47.0 1.0 CB A:SER169 4.3 19.5 1.0 OE1 A:GLU143 4.3 21.6 1.0 O A:HOH648 4.4 44.4 1.0 CD A:GLU143 4.4 25.7 1.0 O A:HOH509 4.4 62.0 1.0 CA A:GLU166 4.6 17.6 1.0 OG A:SER169 4.6 18.1 1.0 O A:HOH593 4.6 37.1 1.0 NE2 A:HIS231 4.7 30.7 1.0 CB A:GLU166 4.8 17.6 1.0 CZ A:TYR157 4.9 25.3 0.4 CE1 A:TYR157 5.0 26.0 0.4

A.C.English, C.R.Groom, R.E.Hubbard. Experimental and Computational Mapping of the Binding Surface of A Crystalline Protein. Protein Eng. V. 14 47 2001.
ISSN: ISSN 0269-2139
PubMed: 11287678
DOI: 10.1093/PROTEIN/14.1.47