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Zinc in PDB 1zkx: Crystal Structure of GLU158ALA/THR159ALA/ASN160ALA- A Triple Mutant of Clostridium Botulinum Neurotoxin E Catalytic Domain

Enzymatic activity of Crystal Structure of GLU158ALA/THR159ALA/ASN160ALA- A Triple Mutant of Clostridium Botulinum Neurotoxin E Catalytic Domain

All present enzymatic activity of Crystal Structure of GLU158ALA/THR159ALA/ASN160ALA- A Triple Mutant of Clostridium Botulinum Neurotoxin E Catalytic Domain:
3.4.24.69;

Protein crystallography data

The structure of Crystal Structure of GLU158ALA/THR159ALA/ASN160ALA- A Triple Mutant of Clostridium Botulinum Neurotoxin E Catalytic Domain, PDB code: 1zkx 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) 46.50 / 2.52
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 88.904, 144.784, 83.017, 90.00, 90.00, 90.00
R / Rfree (%) 20.8 / 25.9

Other elements in 1zkx:

The structure of Crystal Structure of GLU158ALA/THR159ALA/ASN160ALA- A Triple Mutant of Clostridium Botulinum Neurotoxin E Catalytic Domain also contains other interesting chemical elements:

Chlorine (Cl) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of GLU158ALA/THR159ALA/ASN160ALA- A Triple Mutant of Clostridium Botulinum Neurotoxin E Catalytic Domain (pdb code 1zkx). 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 GLU158ALA/THR159ALA/ASN160ALA- A Triple Mutant of Clostridium Botulinum Neurotoxin E Catalytic Domain, PDB code: 1zkx:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1zkx

Go back to Zinc Binding Sites List in 1zkx
Zinc binding site 1 out of 2 in the Crystal Structure of GLU158ALA/THR159ALA/ASN160ALA- A Triple 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 GLU158ALA/THR159ALA/ASN160ALA- A Triple Mutant of Clostridium Botulinum Neurotoxin E Catalytic Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn423

b:32.8
occ:1.00
 OE2 A:GLU250 2.0 35.6 1.0
NE2 A:HIS211 2.1 30.3 1.0
NE2 A:HIS215 2.1 26.5 1.0
CD A:GLU250 2.7 34.7 1.0
OE1 A:GLU250 2.7 37.3 1.0
O A:HOH526 2.8 27.4 1.0
CD2 A:HIS211 2.9 28.1 1.0
CD2 A:HIS215 3.0 24.7 1.0
CE1 A:HIS211 3.2 27.3 1.0
CE1 A:HIS215 3.2 28.6 1.0
OH A:TYR350 4.1 37.6 1.0
CG A:HIS211 4.1 27.2 1.0
OE2 A:GLU212 4.2 28.1 1.0
CG A:GLU250 4.2 32.1 1.0
CE1 A:TYR350 4.2 33.7 1.0
CG A:HIS215 4.2 25.6 1.0
ND1 A:HIS211 4.3 30.1 1.0
ND1 A:HIS215 4.3 27.1 1.0
CZ A:TYR350 4.4 33.8 1.0
OE1 A:GLU212 4.7 26.5 1.0
CB A:GLU250 4.7 29.8 1.0
CD A:GLU212 4.8 25.0 1.0
CA A:GLU250 4.8 28.7 1.0
CG2 A:THR253 4.9 21.2 1.0
O A:HOH491 5.0 40.7 1.0

Zinc binding site 2 out of 2 in 1zkx

Go back to Zinc Binding Sites List in 1zkx
Zinc binding site 2 out of 2 in the Crystal Structure of GLU158ALA/THR159ALA/ASN160ALA- A Triple 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 GLU158ALA/THR159ALA/ASN160ALA- A Triple Mutant of Clostridium Botulinum Neurotoxin E Catalytic Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn822

b:46.3
occ:1.00
 NE2 B:HIS211 1.8 31.6 1.0
NE2 B:HIS215 2.0 39.2 1.0
OE1 B:GLU250 2.1 37.6 1.0
OE2 B:GLU250 2.6 34.5 1.0
CD B:GLU250 2.7 37.6 1.0
CE1 B:HIS211 2.8 32.5 1.0
CD2 B:HIS215 2.8 37.8 1.0
CD2 B:HIS211 2.9 32.0 1.0
O B:HOH935 2.9 34.5 1.0
CE1 B:HIS215 3.2 39.3 1.0
ND1 B:HIS211 4.0 32.1 1.0
CG B:HIS211 4.0 32.3 1.0
CG B:HIS215 4.1 37.5 1.0
CG B:GLU250 4.2 38.0 1.0
ND1 B:HIS215 4.2 38.4 1.0
OH B:TYR350 4.3 53.6 1.0
OE2 B:GLU212 4.5 41.5 1.0
CE1 B:TYR350 4.6 53.7 1.0
CZ B:TYR350 4.7 53.5 1.0
CB B:GLU250 4.8 39.0 1.0
OE1 B:GLU212 4.8 41.4 1.0
CA B:GLU250 4.9 40.4 1.0

Reference:

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
Page generated: Wed Oct 16 21:18:15 2024

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