Zinc in PDB 3qix: Crystal Structure of Bont/A Lc with Zinc Bound

All present enzymatic activity of Crystal Structure of Bont/A Lc with Zinc Bound:
3.4.24.69;

The structure of Crystal Structure of Bont/A Lc with Zinc Bound, PDB code: 3qix was solved by A.A.Thompson, G.W.Han, R.C.Stevens, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.44 / 2.41
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	38.808, 193.747, 56.003, 90.00, 96.12, 90.00
R / Rfree (%)	18.5 / 22.8

The binding sites of Zinc atom in the Crystal Structure of Bont/A Lc with Zinc Bound (pdb code 3qix). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Bont/A Lc with Zinc Bound, PDB code: 3qix:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Bont/A Lc with Zinc Bound


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 Bont/A Lc with Zinc Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1001 b:79.9 occ:1.00 OE1 A:GLU262 2.0 59.1 1.0 NE2 A:HIS223 2.1 33.1 1.0 NE2 A:HIS227 2.1 44.8 1.0 OE2 A:GLU262 2.5 60.2 1.0 CD A:GLU262 2.5 56.0 1.0 CD2 A:HIS227 2.8 40.2 1.0 O A:HOH606 2.8 51.3 1.0 CD2 A:HIS223 3.0 31.6 1.0 CE1 A:HIS223 3.1 31.5 1.0 CE1 A:HIS227 3.4 43.6 1.0 CG A:GLU262 3.9 48.2 1.0 CG A:HIS227 4.0 36.0 1.0 CG A:HIS223 4.2 31.3 1.0 OE2 A:GLU224 4.2 41.8 1.0 ND1 A:HIS223 4.2 32.8 1.0 ND1 A:HIS227 4.3 40.1 1.0 CB A:GLU262 4.7 40.9 1.0 OE1 A:GLU224 4.8 42.0 1.0 CD A:GLU224 4.8 39.3 1.0 OH A:TYR366 4.8 47.9 1.0 CG2 A:THR265 4.9 28.3 1.0 CA A:GLU262 4.9 34.7 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Bont/A Lc with Zinc Bound


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Bont/A Lc with Zinc Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1002 b:91.6 occ:1.00 OE1 B:GLU262 2.0 47.6 1.0 NE2 B:HIS223 2.1 34.2 1.0 NE2 B:HIS227 2.2 48.4 1.0 OE2 B:GLU262 2.6 56.1 1.0 O B:HOH607 2.6 37.3 1.0 CD B:GLU262 2.6 50.0 1.0 CD2 B:HIS223 2.7 31.6 1.0 CD2 B:HIS227 2.9 45.3 1.0 CE1 B:HIS227 3.3 48.7 1.0 CE1 B:HIS223 3.4 33.8 1.0 CG B:HIS223 4.0 29.8 1.0 CG B:HIS227 4.1 42.6 1.0 CG B:GLU262 4.1 43.7 1.0 OE2 B:GLU224 4.2 43.4 1.0 ND1 B:HIS227 4.3 47.0 1.0 ND1 B:HIS223 4.3 36.1 1.0 OH B:TYR366 4.3 58.0 1.0 CE1 B:TYR366 4.6 53.5 1.0 OE1 B:GLU224 4.6 38.6 1.0 CD B:GLU224 4.7 39.4 1.0 CB B:GLU262 4.8 38.9 1.0 CZ B:TYR366 4.9 56.3 1.0

A.A.Thompson, G.S.Jiao, S.Kim, A.Thai, L.Cregar-Hernandez, S.A.Margosiak, A.T.Johnson, G.W.Han, S.O'malley, R.C.Stevens. Structural Characterization of Three Novel Hydroxamate-Based Zinc Chelating Inhibitors of the Clostridium Botulinum Serotype A Neurotoxin Light Chain Metalloprotease Reveals A Compact Binding Site Resulting From 60/70 Loop Flexibility. Biochemistry V. 50 4019 2011.
ISSN: ISSN 0006-2960
PubMed: 21434688
DOI: 10.1021/BI2001483