Zinc in PDB 1f82: Botulinum Neurotoxin Type B Catalytic Domain

All present enzymatic activity of Botulinum Neurotoxin Type B Catalytic Domain:
3.4.24.69;

The structure of Botulinum Neurotoxin Type B Catalytic Domain, PDB code: 1f82 was solved by M.A.Hanson, R.C.Stevens, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.88 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	55.807, 62.684, 130.278, 90.00, 90.00, 90.00
R / Rfree (%)	24.4 / 27.6

The binding sites of Zinc atom in the Botulinum Neurotoxin Type B Catalytic Domain (pdb code 1f82). 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 Botulinum Neurotoxin Type B Catalytic Domain, PDB code: 1f82:

Zinc binding site 1 out of 1 in the Botulinum Neurotoxin Type B Catalytic Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Botulinum Neurotoxin Type B Catalytic Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn500 b:26.8 occ:1.00 O A:HOH833 2.1 32.9 1.0 NE2 A:HIS233 2.1 27.8 1.0 NE2 A:HIS229 2.1 24.2 1.0 OE2 A:GLU267 2.2 26.5 1.0 OE1 A:GLU267 2.6 26.2 1.0 CD A:GLU267 2.7 26.1 1.0 CD2 A:HIS229 2.8 24.5 1.0 CD2 A:HIS233 3.0 24.5 1.0 CE1 A:HIS233 3.1 26.9 1.0 CE1 A:HIS229 3.3 24.3 1.0 OE1 A:GLU230 3.9 31.1 1.0 CG A:HIS229 4.1 25.4 1.0 O A:HOH648 4.1 27.9 1.0 O A:HOH841 4.2 46.3 1.0 CG A:HIS233 4.2 25.8 1.0 ND1 A:HIS233 4.2 26.1 1.0 CG A:GLU267 4.2 27.4 1.0 ND1 A:HIS229 4.3 28.1 1.0 OH A:TYR372 4.3 39.8 1.0 CE2 A:TYR372 4.6 39.2 1.0 CD A:GLU230 4.7 30.1 1.0 CG2 A:THR270 4.8 21.3 1.0 CZ A:TYR372 4.8 39.3 1.0 OE2 A:GLU230 4.8 30.6 1.0 CB A:GLU267 4.9 27.1 1.0 O A:HOH694 4.9 34.3 1.0 CA A:GLU267 5.0 27.4 1.0 CB A:THR270 5.0 22.3 1.0

M.A.Hanson, R.C.Stevens. Cocrystal Structure of Synaptobrevin-II Bound to Botulinum Neurotoxin Type B at 2.0 A Resolution. Nat.Struct.Biol. V. 7 687 2000.
ISSN: ISSN 1072-8368
PubMed: 10932255
DOI: 10.1038/77997