Zinc in PDB 2xhl: Structure of A Functional Derivative of Clostridium Botulinum Neurotoxin Type B

All present enzymatic activity of Structure of A Functional Derivative of Clostridium Botulinum Neurotoxin Type B:
3.4.24.69;

The structure of Structure of A Functional Derivative of Clostridium Botulinum Neurotoxin Type B, PDB code: 2xhl was solved by G.Masuyer, M.Beard, V.A.Cadd, J.A.Chaddock, K.R.Acharya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	113.49 / 2.80
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	66.890, 149.100, 113.490, 90.00, 90.00, 90.00
R / Rfree (%)	23.999 / 28.231

The binding sites of Zinc atom in the Structure of A Functional Derivative of Clostridium Botulinum Neurotoxin Type B (pdb code 2xhl). 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 Structure of A Functional Derivative of Clostridium Botulinum Neurotoxin Type B, PDB code: 2xhl:

Zinc binding site 1 out of 1 in the Structure of A Functional Derivative of Clostridium Botulinum Neurotoxin Type B


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of A Functional Derivative of Clostridium Botulinum Neurotoxin Type B within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1442 b:33.5 occ:1.00 O A:HOH2022 2.1 27.1 1.0 NE2 A:HIS234 2.2 18.7 1.0 NE2 A:HIS230 2.3 21.6 1.0 OE2 A:GLU268 2.3 27.9 1.0 OE1 A:GLU268 2.5 27.6 1.0 CD A:GLU268 2.7 28.1 1.0 CD2 A:HIS234 3.1 18.8 1.0 CD2 A:HIS230 3.2 21.7 1.0 CE1 A:HIS234 3.2 18.5 1.0 CE1 A:HIS230 3.3 21.6 1.0 CG A:HIS234 4.2 19.3 1.0 CG A:GLU268 4.2 27.5 1.0 ND1 A:HIS234 4.3 18.6 1.0 CG A:HIS230 4.4 21.4 1.0 ND1 A:HIS230 4.4 21.5 1.0 OE2 A:GLU231 4.5 23.7 1.0 CG2 A:THR271 4.8 21.8 1.0 OE1 A:GLU231 4.9 24.2 1.0

G.Masuyer, M.Beard, V.A.Cadd, J.A.Chaddock, K.R.Acharya. Structure and Activity of A Functional Derivative of Clostridium Botulinum Neurotoxin B. J.Struct.Biol. V. 174 52 2011.
ISSN: ISSN 1047-8477
PubMed: 21078393
DOI: 10.1016/J.JSB.2010.11.010