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Zinc in PDB 4ktx: Crystal Structure of the Catalytic Domain of Botulinum Neurotoxin Bont/A C134S Mutant with Covalent Inhibitor That Modifies Cys-165 Causing Disorder in 167-174 Stretch

Enzymatic activity of Crystal Structure of the Catalytic Domain of Botulinum Neurotoxin Bont/A C134S Mutant with Covalent Inhibitor That Modifies Cys-165 Causing Disorder in 167-174 Stretch

All present enzymatic activity of Crystal Structure of the Catalytic Domain of Botulinum Neurotoxin Bont/A C134S Mutant with Covalent Inhibitor That Modifies Cys-165 Causing Disorder in 167-174 Stretch:
3.4.24.69;

Protein crystallography data

The structure of Crystal Structure of the Catalytic Domain of Botulinum Neurotoxin Bont/A C134S Mutant with Covalent Inhibitor That Modifies Cys-165 Causing Disorder in 167-174 Stretch, PDB code: 4ktx was solved by E.A.Stura, L.Vera, K.Guitot, V.Dive, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.80 / 2.59
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 65.410, 65.410, 200.970, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 29.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Catalytic Domain of Botulinum Neurotoxin Bont/A C134S Mutant with Covalent Inhibitor That Modifies Cys-165 Causing Disorder in 167-174 Stretch (pdb code 4ktx). 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 Crystal Structure of the Catalytic Domain of Botulinum Neurotoxin Bont/A C134S Mutant with Covalent Inhibitor That Modifies Cys-165 Causing Disorder in 167-174 Stretch, PDB code: 4ktx:

Zinc binding site 1 out of 1 in 4ktx

Go back to Zinc Binding Sites List in 4ktx
Zinc binding site 1 out of 1 in the Crystal Structure of the Catalytic Domain of Botulinum Neurotoxin Bont/A C134S Mutant with Covalent Inhibitor That Modifies Cys-165 Causing Disorder in 167-174 Stretch


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 the Catalytic Domain of Botulinum Neurotoxin Bont/A C134S Mutant with Covalent Inhibitor That Modifies Cys-165 Causing Disorder in 167-174 Stretch within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:32.0
occ:1.00
 O B:DPP2 1.8 25.7 1.0
NE2 A:HIS227 2.1 24.8 1.0
N B:DPP2 2.1 34.9 1.0
OE1 A:GLU262 2.2 28.6 1.0
NE2 A:HIS223 2.3 28.7 1.0
C B:DPP2 2.5 28.9 1.0
OE2 A:GLU262 2.8 23.5 1.0
CA B:DPP2 2.8 25.7 1.0
CD A:GLU262 2.8 28.8 1.0
CD2 A:HIS227 3.0 30.1 1.0
CE1 A:HIS227 3.1 27.5 1.0
CD2 A:HIS223 3.2 25.7 1.0
CE1 A:HIS223 3.3 20.8 1.0
CB B:DPP2 3.7 36.7 1.0
N B:ARG3 3.9 30.2 1.0
O A:HOH618 3.9 32.2 1.0
CG A:HIS227 4.1 34.4 1.0
ND1 A:HIS227 4.1 23.8 1.0
CG A:GLU262 4.3 28.5 1.0
ND1 A:HIS223 4.4 38.3 1.0
CG A:HIS223 4.4 35.2 1.0
CA B:ARG3 4.5 24.8 1.0
OH A:TYR366 4.5 24.1 1.0
CE1 A:TYR366 4.6 25.3 1.0
OE2 A:GLU224 4.6 31.9 1.0
NG B:DPP2 4.7 42.7 1.0
O B:HOH101 4.7 34.1 1.0
CG2 A:THR265 4.7 34.3 1.0
CB A:GLU262 4.9 28.0 1.0
CZ A:TYR366 5.0 31.4 1.0

Reference:

K.Guitot, L.Vera, L.Le Roux, S.Bregant, D.Ptchelkine, F.Beau, E.A.Stura, V.Dive. Covalent Modification of the Active Site Cysteine Stresses Clostridium Botulinum Neurotoxin A To Be Published.
Page generated: Sun Oct 27 01:21:44 2024

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