Zinc in PDB 3qgv: Crystal Structure of A Thermostable Amylase Variant

All present enzymatic activity of Crystal Structure of A Thermostable Amylase Variant:
3.2.1.1;

The structure of Crystal Structure of A Thermostable Amylase Variant, PDB code: 3qgv was solved by K.L.Hein, G.Ganshaw, R.Bott, P.Nissen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.10
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	59.900, 59.900, 272.410, 90.00, 90.00, 90.00
R / Rfree (%)	16.5 / 20.7

The structure of Crystal Structure of A Thermostable Amylase Variant also contains other interesting chemical elements:

Calcium

(Ca)

4 atoms

The binding sites of Zinc atom in the Crystal Structure of A Thermostable Amylase Variant (pdb code 3qgv). 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 A Thermostable Amylase Variant, PDB code: 3qgv:

Zinc binding site 1 out of 1 in the Crystal Structure of A Thermostable Amylase Variant


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 A Thermostable Amylase Variant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn500 b:33.5 occ:1.00 NE2 A:HIS152 2.0 42.5 1.0 O A:HOH605 2.1 33.0 1.0 NE2 A:HIS147 2.1 34.9 1.0 SG A:CYS166 2.3 28.5 1.0 CE1 A:HIS152 2.9 47.1 1.0 CD2 A:HIS147 3.0 34.5 1.0 CD2 A:HIS152 3.1 43.5 1.0 CB A:CYS166 3.1 28.1 1.0 CE1 A:HIS147 3.2 41.8 1.0 CA A:CYS166 3.4 34.3 1.0 OD2 A:ASP168 3.8 39.2 1.0 ND1 A:HIS152 4.1 50.6 1.0 C A:CYS166 4.1 34.1 1.0 CG A:HIS152 4.2 40.6 1.0 CG A:HIS147 4.2 40.2 1.0 ND1 A:HIS147 4.3 38.0 1.0 CB A:ASP168 4.3 36.1 1.0 O A:HOH633 4.3 25.1 1.0 N A:HIS167 4.4 28.9 1.0 N A:ASP168 4.5 29.7 1.0 CG A:ASP168 4.6 40.8 1.0 N A:CYS166 4.6 36.6 1.0 ND2 A:ASN149 4.7 29.0 1.0 O A:CYS166 4.9 32.3 1.0 O A:ILE165 4.9 31.3 1.0

K.L.Hein, G.Ganshaw, R.Bott, P.Nissen. Structure of A Highly Mutated, Thermostable \Xce\XB1-Amylase Variant To Be Published.