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Zinc in PDB 4elc: Crystal Structure of the Catalytic Domain of Botulinum Neurotoxin Bont/A C134 Mutant with Mtsea Modified Cys-165

Enzymatic activity of Crystal Structure of the Catalytic Domain of Botulinum Neurotoxin Bont/A C134 Mutant with Mtsea Modified Cys-165

All present enzymatic activity of Crystal Structure of the Catalytic Domain of Botulinum Neurotoxin Bont/A C134 Mutant with Mtsea Modified Cys-165:
3.4.24.69;

Protein crystallography data

The structure of Crystal Structure of the Catalytic Domain of Botulinum Neurotoxin Bont/A C134 Mutant with Mtsea Modified Cys-165, PDB code: 4elc was solved by E.A.Stura, L.Vera, D.Ptchelkine, H.Bakirci, S.Garcia, V.Dive, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.95 / 1.80
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 65.290, 65.290, 200.910, 90.00, 90.00, 90.00
R / Rfree (%) 16.9 / 22.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Catalytic Domain of Botulinum Neurotoxin Bont/A C134 Mutant with Mtsea Modified Cys-165 (pdb code 4elc). 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 C134 Mutant with Mtsea Modified Cys-165, PDB code: 4elc:

Zinc binding site 1 out of 1 in 4elc

Go back to Zinc Binding Sites List in 4elc
Zinc binding site 1 out of 1 in the Crystal Structure of the Catalytic Domain of Botulinum Neurotoxin Bont/A C134 Mutant with Mtsea Modified Cys-165


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 C134 Mutant with Mtsea Modified Cys-165 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:11.5
occ:1.00
 OE1 A:GLU262 2.0 10.9 1.0
O1A A:LMR504 2.0 13.9 1.0
NE2 A:HIS223 2.1 15.0 1.0
NE2 A:HIS227 2.1 8.2 1.0
O2 A:LMR504 2.2 18.9 1.0
CD A:GLU262 2.6 14.2 1.0
OE2 A:GLU262 2.6 15.0 1.0
C1 A:LMR504 2.8 23.3 1.0
CD2 A:HIS223 3.0 10.8 1.0
CD2 A:HIS227 3.0 6.9 1.0
C2 A:LMR504 3.0 21.5 1.0
CE1 A:HIS223 3.2 13.3 1.0
CE1 A:HIS227 3.2 10.3 1.0
O A:HOH1018 4.0 38.6 1.0
C3 A:LMR504 4.0 25.5 1.0
O1B A:LMR504 4.1 21.1 1.0
CG A:GLU262 4.1 12.1 1.0
CG A:HIS223 4.2 9.2 1.0
CG A:HIS227 4.2 10.9 1.0
ND1 A:HIS223 4.2 11.0 1.0
OH A:TYR366 4.2 16.9 1.0
ND1 A:HIS227 4.2 10.3 1.0
CE1 A:TYR366 4.3 13.5 1.0
N3 A:0QL165 4.5 23.6 1.0
CZ A:TYR366 4.6 11.7 1.0
CB A:GLU262 4.7 9.6 1.0
CG2 A:THR265 4.7 9.1 1.0
O A:HOH1077 4.7 54.5 1.0
OE1 A:GLU224 4.8 20.4 1.0
C4 A:LMR504 4.9 29.8 1.0
CA A:GLU262 4.9 10.4 1.0

Reference:

E.A.Stura, L.Le Roux, K.Guitot, S.Garcia, S.Bregant, F.Beau, L.Vera, G.Collet, D.Ptchelkine, H.Bakirci, V.Dive. Structural Framework For Covalent Inhibition of Clostridium Botulinum Neurotoxin A By Targeting CYS165. J.Biol.Chem. V. 287 33607 2012.
ISSN: ISSN 0021-9258
PubMed: 22869371
DOI: 10.1074/JBC.M112.396697
Page generated: Sat Oct 26 22:01:57 2024

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