Zinc in PDB 1zkw: Crystal Structure of ARG347ALA Mutant of Botulinum Neurotoxin E Catalytic Domain

All present enzymatic activity of Crystal Structure of ARG347ALA Mutant of Botulinum Neurotoxin E Catalytic Domain:
3.4.24.69;

The structure of Crystal Structure of ARG347ALA Mutant of Botulinum Neurotoxin E Catalytic Domain, PDB code: 1zkw 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)	42.35 / 2.17
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	88.581, 144.458, 82.706, 90.00, 90.00, 90.00
R / Rfree (%)	23.8 / 28

The structure of Crystal Structure of ARG347ALA Mutant of Botulinum Neurotoxin E Catalytic Domain also contains other interesting chemical elements:

Chlorine

(Cl)

7 atoms

The binding sites of Zinc atom in the Crystal Structure of ARG347ALA Mutant of Botulinum Neurotoxin E Catalytic Domain (pdb code 1zkw). 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 ARG347ALA Mutant of Botulinum Neurotoxin E Catalytic Domain, PDB code: 1zkw:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of ARG347ALA Mutant of 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 ARG347ALA Mutant of Botulinum Neurotoxin E Catalytic Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn422 b:34.2 occ:1.00 NE2 A:HIS215 2.1 17.3 1.0 OE2 A:GLU250 2.2 30.1 1.0 NE2 A:HIS211 2.3 22.4 1.0 O A:HOH745 2.6 29.5 1.0 CD2 A:HIS215 3.0 17.6 1.0 CD A:GLU250 3.0 30.0 1.0 CD2 A:HIS211 3.0 21.7 1.0 CE1 A:HIS215 3.1 18.2 1.0 OE1 A:GLU250 3.1 34.0 1.0 CE1 A:HIS211 3.5 22.2 1.0 CE1 A:TYR350 3.8 31.9 1.0 OE2 A:GLU212 3.9 22.8 1.0 OH A:TYR350 4.0 35.5 1.0 CZ A:TYR350 4.1 32.8 1.0 CG A:HIS215 4.2 18.8 1.0 ND1 A:HIS215 4.2 20.5 1.0 CG A:HIS211 4.3 21.9 1.0 CG A:GLU250 4.5 28.7 1.0 ND1 A:HIS211 4.5 24.5 1.0 CD1 A:TYR350 4.6 30.8 1.0 OE1 A:GLU212 4.6 24.9 1.0 CD A:GLU212 4.7 21.8 1.0 O A:HOH639 4.7 17.1 1.0 CA A:GLU250 4.8 25.9 1.0 CG2 A:THR253 4.8 18.5 1.0 CB A:GLU250 4.9 26.1 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of ARG347ALA Mutant of 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 ARG347ALA Mutant of Botulinum Neurotoxin E Catalytic Domain within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn822 b:49.2 occ:1.00 NE2 B:HIS211 2.1 30.6 1.0 NE2 B:HIS215 2.1 37.9 1.0 OE1 B:GLU250 2.2 43.7 1.0 O B:HOH920 2.5 28.7 1.0 CD2 B:HIS215 3.0 36.7 1.0 CE1 B:HIS211 3.1 31.4 1.0 CD2 B:HIS211 3.1 31.0 1.0 CE1 B:HIS215 3.1 37.4 1.0 CD B:GLU250 3.3 42.8 1.0 OH B:TYR350 3.5 56.0 1.0 OE2 B:GLU250 3.7 44.9 1.0 CE1 B:TYR350 3.8 57.7 1.0 CZ B:TYR350 4.0 57.2 1.0 ND1 B:HIS211 4.2 29.7 1.0 CG B:HIS215 4.2 35.0 1.0 ND1 B:HIS215 4.2 37.3 1.0 CG B:HIS211 4.2 30.9 1.0 OE2 B:GLU212 4.5 35.7 1.0 CG B:GLU250 4.5 42.2 1.0 CA B:GLU250 4.7 37.8 1.0 CB B:GLU250 4.7 39.5 1.0 CG2 B:THR253 4.9 34.4 1.0 CD1 B:TYR350 4.9 58.4 1.0 CB B:THR253 5.0 35.7 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