Zinc in PDB 1zn3: Crystal Structure of GLU335ALA Mutant of Clostridium Botulinum Neurotoxin Type E

All present enzymatic activity of Crystal Structure of GLU335ALA Mutant of Clostridium Botulinum Neurotoxin Type E:
3.4.24.69;

The structure of Crystal Structure of GLU335ALA Mutant of Clostridium Botulinum Neurotoxin Type E, PDB code: 1zn3 was solved by R.Agarwal, T.Binz, S.Swaminathan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.57 / 2.60
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	89.090, 144.720, 83.230, 90.00, 90.00, 90.00
R / Rfree (%)	22 / 25.9

The structure of Crystal Structure of GLU335ALA Mutant of Clostridium Botulinum Neurotoxin Type E also contains other interesting chemical elements:

Chlorine

(Cl)

5 atoms

The binding sites of Zinc atom in the Crystal Structure of GLU335ALA Mutant of Clostridium Botulinum Neurotoxin Type E (pdb code 1zn3). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of GLU335ALA Mutant of Clostridium Botulinum Neurotoxin Type E, PDB code: 1zn3:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of GLU335ALA Mutant of Clostridium Botulinum Neurotoxin Type E


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 GLU335ALA Mutant of Clostridium Botulinum Neurotoxin Type E within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn422 b:49.6 occ:1.00 NE2 A:HIS215 2.3 26.2 1.0 OE2 A:GLU250 2.4 38.7 1.0 NE2 A:HIS211 2.4 30.6 1.0 O A:HOH505 2.5 49.5 1.0 CD2 A:HIS215 3.0 27.0 1.0 CD2 A:HIS211 3.1 30.6 1.0 CD A:GLU250 3.4 37.6 1.0 OE2 A:GLU212 3.4 32.9 1.0 CE1 A:HIS215 3.5 26.7 1.0 CE1 A:HIS211 3.5 30.9 1.0 OE1 A:GLU250 3.8 40.0 1.0 O A:HOH576 4.2 36.9 1.0 CE1 A:TYR350 4.2 43.4 1.0 OE1 A:GLU212 4.2 32.4 1.0 CD A:GLU212 4.2 30.4 1.0 CG A:HIS215 4.3 27.4 1.0 CG A:HIS211 4.4 29.1 1.0 ND1 A:HIS215 4.5 27.0 1.0 ND1 A:HIS211 4.5 31.3 1.0 CG A:GLU250 4.7 36.3 1.0 CD1 A:TYR350 4.8 41.0 1.0 CZ A:TYR350 4.8 45.0 1.0 OH A:TYR350 4.9 46.8 1.0 CG2 A:THR253 5.0 27.2 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of GLU335ALA Mutant of Clostridium Botulinum Neurotoxin Type E


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of GLU335ALA Mutant of Clostridium Botulinum Neurotoxin Type E within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn822 b:71.2 occ:1.00 OE1 B:GLU250 2.2 44.5 1.0 NE2 B:HIS215 2.2 45.2 1.0 NE2 B:HIS211 2.3 44.4 1.0 O B:HOH823 2.5 47.9 0.5 CE1 B:HIS215 3.2 43.8 1.0 CD B:GLU250 3.2 44.5 1.0 CD2 B:HIS215 3.3 42.9 1.0 CE1 B:HIS211 3.3 44.3 1.0 CD2 B:HIS211 3.3 43.0 1.0 OE2 B:GLU250 3.5 45.4 1.0 CE1 B:TYR350 4.2 55.0 1.0 ND1 B:HIS215 4.3 43.1 1.0 OE2 B:GLU212 4.4 37.0 1.0 CG B:HIS215 4.4 42.2 1.0 ND1 B:HIS211 4.4 42.7 1.0 CG B:HIS211 4.4 40.5 1.0 CG B:GLU250 4.6 43.9 1.0 OH B:TYR350 4.6 54.0 1.0 CZ B:TYR350 4.7 55.4 1.0 CA B:GLU250 4.7 43.4 1.0 CB B:GLU250 4.8 44.1 1.0 CD1 B:TYR350 4.9 56.8 1.0 CG2 B:THR253 5.0 42.1 1.0 CB B:THR253 5.0 43.3 1.0

R.Agarwal, T.Binz, S.Swaminathan. Analysis of Active Site Residues of Botulinum Neurotoxin E By Mutational, Functional, and Structural Studies: GLU335GLN Is An Apoenzyme. Biochemistry V. 44 8291 2005.
ISSN: ISSN 0006-2960
PubMed: 15938619
DOI: 10.1021/BI050253A