Zinc in PDB 1zl6: Crystal Structure of TYR350ALA Mutant of Clostridium Botulinum Neurotoxin E Catalytic Domain

All present enzymatic activity of Crystal Structure of TYR350ALA Mutant of Clostridium Botulinum Neurotoxin E Catalytic Domain:
3.4.24.69;

The structure of Crystal Structure of TYR350ALA Mutant of Clostridium Botulinum Neurotoxin E Catalytic Domain, PDB code: 1zl6 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)	46.54 / 2.40
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	88.800, 144.958, 83.185, 90.00, 90.00, 90.00
R / Rfree (%)	23.5 / 28.4

The binding sites of Zinc atom in the Crystal Structure of TYR350ALA Mutant of Clostridium Botulinum Neurotoxin E Catalytic Domain (pdb code 1zl6). 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 TYR350ALA Mutant of Clostridium Botulinum Neurotoxin E Catalytic Domain, PDB code: 1zl6:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of TYR350ALA Mutant of Clostridium Botulinum Neurotoxin E Catalytic Domain


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 TYR350ALA Mutant of Clostridium Botulinum Neurotoxin E Catalytic Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn422 b:48.6 occ:1.00 NE2 A:HIS211 2.0 35.1 1.0 NE2 A:HIS215 2.1 31.2 1.0 O1 A:SO4500 2.4 57.4 1.0 OE1 A:GLU250 2.5 49.3 1.0 O3 A:SO4500 2.6 58.3 1.0 OE2 A:GLU250 2.8 51.7 1.0 CD A:GLU250 3.0 49.6 1.0 CD2 A:HIS211 3.0 34.8 1.0 CD2 A:HIS215 3.0 29.1 1.0 S A:SO4500 3.1 62.2 1.0 CE1 A:HIS211 3.1 35.9 1.0 CE1 A:HIS215 3.2 29.4 1.0 O4 A:SO4500 4.0 61.9 1.0 O2 A:SO4500 4.2 60.7 1.0 ND1 A:HIS211 4.2 37.6 1.0 CG A:HIS211 4.2 35.0 1.0 CG A:HIS215 4.2 28.9 1.0 ND1 A:HIS215 4.3 29.1 1.0 CG A:GLU250 4.4 48.4 1.0 OE2 A:GLU212 4.5 42.3 1.0 CG2 A:THR253 4.7 36.3 1.0 CA A:GLU250 4.8 42.9 1.0 OE1 A:GLU212 5.0 36.9 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of TYR350ALA Mutant of Clostridium Botulinum Neurotoxin E Catalytic Domain


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 TYR350ALA Mutant of Clostridium Botulinum Neurotoxin E Catalytic Domain within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn822 b:67.5 occ:1.00 NE2 B:HIS215 2.1 60.4 1.0 NE2 B:HIS211 2.1 47.1 1.0 OE1 B:GLU250 2.4 68.0 1.0 CD2 B:HIS211 2.7 45.6 1.0 CD2 B:HIS215 2.7 58.8 1.0 OE2 B:GLU250 2.7 68.0 1.0 CD B:GLU250 2.8 67.7 1.0 CE1 B:HIS211 3.2 48.6 1.0 O B:HOH826 3.2 53.2 1.0 CE1 B:HIS215 3.3 60.2 1.0 CG B:HIS211 3.9 47.6 1.0 CG B:HIS215 4.0 56.8 1.0 CG B:GLU250 4.0 65.9 1.0 OE2 B:GLU212 4.1 58.1 1.0 ND1 B:HIS211 4.1 48.5 1.0 ND1 B:HIS215 4.2 60.2 1.0 O B:HOH883 4.7 53.2 1.0 CG2 B:THR253 4.8 53.8 1.0 CB B:GLU250 4.8 64.1 1.0 CD B:GLU212 4.9 57.0 1.0 CA B:GLU250 4.9 62.0 1.0 O B:HIS211 4.9 50.5 1.0 CB B:THR253 5.0 55.0 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