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Zinc in PDB 8ow8: Crystal Structure of the Catalytic Domain of A Botulinum Neurotoxin Homologue From Enterococcus Faecium

Enzymatic activity of Crystal Structure of the Catalytic Domain of A Botulinum Neurotoxin Homologue From Enterococcus Faecium

All present enzymatic activity of Crystal Structure of the Catalytic Domain of A Botulinum Neurotoxin Homologue From Enterococcus Faecium:
3.4.24.69;

Protein crystallography data

The structure of Crystal Structure of the Catalytic Domain of A Botulinum Neurotoxin Homologue From Enterococcus Faecium, PDB code: 8ow8 was solved by K.S.Gregory, K.R.Acharya, S.M.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 64.43 / 2.00
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 143.894, 143.894, 51.695, 90, 90, 90
R / Rfree (%) 18.8 / 22.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Catalytic Domain of A Botulinum Neurotoxin Homologue From Enterococcus Faecium (pdb code 8ow8). 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 A Botulinum Neurotoxin Homologue From Enterococcus Faecium, PDB code: 8ow8:

Zinc binding site 1 out of 1 in 8ow8

Go back to Zinc Binding Sites List in 8ow8
Zinc binding site 1 out of 1 in the Crystal Structure of the Catalytic Domain of A Botulinum Neurotoxin Homologue From Enterococcus Faecium


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 A Botulinum Neurotoxin Homologue From Enterococcus Faecium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:48.2
occ:1.00
 HE2 A:HIS225 1.1 30.0 0.0
HE2 A:HIS229 1.2 30.0 0.0
O2 A:PO4503 1.7 47.1 1.0
NE2 A:HIS225 2.0 46.0 1.0
OE1 A:GLU269 2.0 54.3 1.0
NE2 A:HIS229 2.1 45.4 1.0
OE2 A:GLU269 2.5 47.2 1.0
CD A:GLU269 2.6 50.8 1.0
CE1 A:HIS225 3.0 48.8 1.0
CE1 A:HIS229 3.0 48.8 1.0
P A:PO4503 3.0 63.4 1.0
CD2 A:HIS225 3.0 49.1 1.0
CD2 A:HIS229 3.1 39.0 1.0
HE1 A:HIS229 3.2 47.6 1.0
HE1 A:HIS225 3.2 49.2 1.0
HD2 A:HIS225 3.2 46.4 1.0
HD2 A:HIS229 3.3 41.3 1.0
O3 A:PO4503 3.3 59.2 1.0
HE1 A:TYR367 3.5 57.7 1.0
HH A:TYR367 3.6 30.0 0.0
O A:HOH719 3.9 50.6 1.0
O1 A:PO4503 3.9 54.9 1.0
HA A:GLU269 3.9 47.4 1.0
CE1 A:TYR367 4.1 60.2 1.0
CG A:GLU269 4.1 50.2 1.0
ND1 A:HIS225 4.1 49.3 1.0
ND1 A:HIS229 4.2 43.6 1.0
CG A:HIS225 4.2 44.8 1.0
OH A:TYR367 4.2 55.8 1.0
O4 A:PO4503 4.2 59.2 1.0
CG A:HIS229 4.2 45.9 1.0
HG21 A:THR272 4.3 46.6 1.0
OE1 A:GLU226 4.3 51.8 1.0
HB A:THR272 4.4 49.1 1.0
CZ A:TYR367 4.5 55.2 1.0
HG3 A:GLU269 4.5 50.6 1.0
HG23 A:THR272 4.5 47.4 1.0
HG2 A:GLU269 4.6 50.4 1.0
CG2 A:THR272 4.8 47.0 1.0
CA A:GLU269 4.8 46.6 1.0
HB3 A:GLU269 4.8 49.8 1.0
CB A:GLU269 4.8 50.2 1.0
OE2 A:GLU226 4.9 54.0 1.0
CD A:GLU226 4.9 48.7 1.0
HD1 A:HIS225 4.9 30.0 0.0
HD1 A:HIS229 5.0 30.0 0.0

Reference:

K.S.Gregory, P.R.Hall, J.P.Onuh, O.O.Mojanaga, S.M.Liu, K.R.Acharya. Crystal Structure of the Catalytic Domain of A Botulinum Neurotoxin Homologue From Enterococcus Faecium: Potential Insights Into Substrate Recognition Int J Mol Sci 2023.
ISSN: ESSN 1422-0067
DOI: 10.3390/IJMS241612721
Page generated: Thu Oct 31 09:02:38 2024

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