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Zinc in PDB 3fii: Crystal Structure of Clostridium Botulinum Neurotoxin Serotype F Catalytic Domain with An Inhibitor (INH2)

Enzymatic activity of Crystal Structure of Clostridium Botulinum Neurotoxin Serotype F Catalytic Domain with An Inhibitor (INH2)

All present enzymatic activity of Crystal Structure of Clostridium Botulinum Neurotoxin Serotype F Catalytic Domain with An Inhibitor (INH2):
3.4.24.69;

Protein crystallography data

The structure of Crystal Structure of Clostridium Botulinum Neurotoxin Serotype F Catalytic Domain with An Inhibitor (INH2), PDB code: 3fii was solved by R.Agarwal, S.Swaminathan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.76 / 2.17
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 55.592, 70.353, 113.929, 90.00, 90.00, 90.00
R / Rfree (%) 24.6 / 29

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Clostridium Botulinum Neurotoxin Serotype F Catalytic Domain with An Inhibitor (INH2) (pdb code 3fii). 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 Clostridium Botulinum Neurotoxin Serotype F Catalytic Domain with An Inhibitor (INH2), PDB code: 3fii:

Zinc binding site 1 out of 1 in 3fii

Go back to Zinc Binding Sites List in 3fii
Zinc binding site 1 out of 1 in the Crystal Structure of Clostridium Botulinum Neurotoxin Serotype F Catalytic Domain with An Inhibitor (INH2)


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 Clostridium Botulinum Neurotoxin Serotype F Catalytic Domain with An Inhibitor (INH2) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn822

b:53.5
occ:1.00
 OE1 A:GLU266 2.1 34.4 1.0
NE2 A:HIS231 2.2 29.2 1.0
SG B:00C58 2.3 51.7 1.0
NE2 A:HIS227 2.3 34.4 1.0
OD1 B:00C58 2.4 50.9 1.0
OE2 A:GLU266 2.6 33.1 1.0
CD A:GLU266 2.6 33.1 1.0
CE1 A:HIS231 3.2 27.4 1.0
CD2 A:HIS231 3.2 29.4 1.0
CD2 A:HIS227 3.2 34.3 1.0
OD2 B:00C58 3.4 51.6 1.0
CE1 A:HIS227 3.4 36.0 1.0
N B:00C58 3.7 46.9 1.0
CB B:00C58 3.7 49.3 1.0
CA B:00C58 4.0 47.9 1.0
CG A:GLU266 4.1 30.4 1.0
OH A:TYR368 4.2 30.5 1.0
O A:HOH1199 4.3 36.6 1.0
ND1 A:HIS231 4.3 28.6 1.0
CG A:HIS231 4.3 29.2 1.0
CG A:HIS227 4.4 33.4 1.0
CE1 A:TYR368 4.4 29.1 1.0
C B:ASP57 4.4 46.5 1.0
ND1 A:HIS227 4.5 34.3 1.0
CB B:ASP57 4.6 46.6 1.0
CZ A:TYR368 4.7 29.7 1.0
OE2 A:GLU228 4.7 33.8 1.0
CB A:GLU266 4.8 29.2 1.0
CA A:GLU266 4.9 28.9 1.0
CA B:ASP57 4.9 46.7 1.0
CG2 A:THR269 5.0 27.2 1.0
OE1 A:GLU228 5.0 37.1 1.0

Reference:

R.Agarwal, J.J.Schmidt, R.G.Stafford, S.Swaminathan. Mode of Vamp Substrate Recognition and Inhibition of Clostridium Botulinum Neurotoxin F. Nat.Struct.Mol.Biol. V. 16 789 2009.
ISSN: ISSN 1545-9993
PubMed: 19543288
DOI: 10.1038/NSMB.1626
Page generated: Thu Oct 24 13:14:03 2024

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