Zinc in PDB 2ise: Botulinum Neurotoxin A Light Chain Wt Crystal Form A

The structure of Botulinum Neurotoxin A Light Chain Wt Crystal Form A, PDB code: 2ise was solved by A.T.Brunger, C.M.Stegmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.35 / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	57.094, 189.407, 39.626, 90.00, 90.00, 90.00
R / Rfree (%)	24.2 / 29.9

The binding sites of Zinc atom in the Botulinum Neurotoxin A Light Chain Wt Crystal Form A (pdb code 2ise). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Botulinum Neurotoxin A Light Chain Wt Crystal Form A, PDB code: 2ise:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Botulinum Neurotoxin A Light Chain Wt Crystal Form A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Botulinum Neurotoxin A Light Chain Wt Crystal Form A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn500 b:39.0 occ:1.00 NE2 A:HIS223 1.9 24.1 1.0 OE1 A:GLU262 2.1 39.0 1.0 NE2 A:HIS227 2.1 27.0 1.0 CE1 A:HIS223 2.8 24.0 1.0 CD A:GLU262 2.8 42.1 1.0 OE2 A:GLU262 2.9 40.5 1.0 CD2 A:HIS227 3.0 27.2 1.0 CD2 A:HIS223 3.0 26.1 1.0 CE1 A:HIS227 3.2 26.8 1.0 ND1 A:HIS223 4.0 25.5 1.0 CG A:HIS223 4.1 25.6 1.0 CG A:HIS227 4.2 28.0 1.0 ND1 A:HIS227 4.2 27.8 1.0 CG A:GLU262 4.3 39.1 1.0 CE2 A:TYR366 4.3 73.2 1.0 OH A:TYR366 4.4 74.5 1.0 OE2 A:GLU224 4.7 36.3 1.0 OE1 A:GLU224 4.8 39.1 1.0 CA A:GLU262 4.8 33.0 1.0 CZ A:TYR366 4.8 74.0 1.0 CG2 A:THR265 4.8 31.9 1.0 CB A:GLU262 4.9 36.0 1.0

Zinc binding site 2 out of 2 in the Botulinum Neurotoxin A Light Chain Wt Crystal Form A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Botulinum Neurotoxin A Light Chain Wt Crystal Form A within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn501 b:38.0 occ:1.00 NE2 B:HIS223 2.0 24.6 1.0 OE1 B:GLU262 2.1 32.6 1.0 NE2 B:HIS227 2.2 21.9 1.0 O B:HOH552 2.6 35.0 1.0 OE2 B:GLU262 2.6 37.5 1.0 CD B:GLU262 2.7 37.8 1.0 CE1 B:HIS223 2.8 23.6 1.0 CD2 B:HIS227 3.0 21.4 1.0 CD2 B:HIS223 3.0 24.8 1.0 CE1 B:HIS227 3.2 19.6 1.0 OH B:TYR366 4.0 76.3 1.0 ND1 B:HIS223 4.0 26.2 1.0 CG B:HIS223 4.1 25.2 1.0 CG B:GLU262 4.2 36.9 1.0 CG B:HIS227 4.2 23.5 1.0 CE2 B:TYR366 4.2 75.8 1.0 ND1 B:HIS227 4.3 22.6 1.0 CZ B:TYR366 4.5 76.0 1.0 OE1 B:GLU224 4.6 35.8 1.0 CA B:GLU262 4.8 31.9 1.0 CG2 B:THR265 4.8 27.1 1.0 CB B:GLU262 4.8 36.1 1.0 OE2 B:GLU224 4.9 34.7 1.0

J.C.Burnett, G.Ruthel, C.M.Stegmann, R.G.Panchal, T.L.Nguyen, A.R.Hermone, R.G.Stafford, D.J.Lane, T.A.Kenny, C.F.Mcgrath, P.Wipf, A.M.Stahl, J.J.Schmidt, R.Gussio, A.T.Brunger, S.Bavari. Inhibition of Metalloprotease Botulinum Serotype A From A Pseudo-Peptide Binding Mode to A Small Molecule That Is Active in Primary Neurons. J.Biol.Chem. V. 282 5004 2007.
ISSN: ISSN 0021-9258
PubMed: 17092934
DOI: 10.1074/JBC.M608166200