Zinc in PDB 6s9a: Artificial Gtpase-Bse Dimer of Human DYNAMIN1

All present enzymatic activity of Artificial Gtpase-Bse Dimer of Human DYNAMIN1:
3.6.5.5;

The structure of Artificial Gtpase-Bse Dimer of Human DYNAMIN1, PDB code: 6s9a was solved by O.M.Ganichkin, R.Vancraenenbroeck, G.Rosenblum, H.Hofmann, O.Daumke, J.K.Noel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.73 / 1.86
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	70.693, 69.546, 74.277, 90.00, 113.15, 90.00
R / Rfree (%)	21.9 / 25.5

The structure of Artificial Gtpase-Bse Dimer of Human DYNAMIN1 also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Zinc atom in the Artificial Gtpase-Bse Dimer of Human DYNAMIN1 (pdb code 6s9a). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Artificial Gtpase-Bse Dimer of Human DYNAMIN1, PDB code: 6s9a:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Artificial Gtpase-Bse Dimer of Human DYNAMIN1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Artificial Gtpase-Bse Dimer of Human DYNAMIN1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn801 b:45.7 occ:1.00 O B:HOH952 1.9 42.9 1.0 NE2 A:HIS142 1.9 45.4 1.0 OD2 A:ASP185 2.0 43.2 1.0 NE2 B:HIS183 2.0 45.2 1.0 CG A:ASP185 2.7 39.6 1.0 OD1 A:ASP185 2.8 41.8 1.0 CE1 A:HIS142 2.9 43.6 1.0 CE1 B:HIS183 2.9 46.1 1.0 CD2 A:HIS142 2.9 45.0 1.0 CD2 B:HIS183 3.0 41.7 1.0 OD2 B:ASP180 4.0 48.0 1.0 ND1 A:HIS142 4.0 47.1 1.0 O A:HOH931 4.1 47.4 1.0 ND1 B:HIS183 4.1 42.5 1.0 CG A:HIS142 4.1 46.6 1.0 O A:HOH921 4.1 44.4 1.0 CG B:HIS183 4.1 40.6 1.0 CB A:ASP185 4.2 39.7 1.0 O A:MET140 4.3 42.5 1.0 CA A:GLY39 4.6 40.6 1.0 CG B:ASP180 4.7 45.0 1.0 CB B:ASP180 4.8 45.2 1.0 CL A:CL803 4.9 45.5 1.0 C A:MET140 4.9 43.6 1.0

Zinc binding site 2 out of 4 in the Artificial Gtpase-Bse Dimer of Human DYNAMIN1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Artificial Gtpase-Bse Dimer of Human DYNAMIN1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn802 b:83.7 occ:0.50 ND1 A:HIS733 1.9 0.4 1.0 O A:HOH956 2.0 83.5 1.0 O A:HOH920 2.0 84.9 1.0 CG A:HIS733 2.8 0.3 1.0 CE1 A:HIS733 2.9 0.6 1.0 CB A:HIS733 3.1 0.5 1.0 CA A:HIS733 3.8 0.4 1.0 CD2 A:HIS733 3.9 0.7 1.0 NE2 A:HIS733 3.9 0.6 1.0 C A:HIS733 4.7 95.4 1.0 O A:HIS733 4.7 95.5 1.0 N A:HIS733 4.9 98.7 1.0

Zinc binding site 3 out of 4 in the Artificial Gtpase-Bse Dimer of Human DYNAMIN1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Artificial Gtpase-Bse Dimer of Human DYNAMIN1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn801 b:45.9 occ:1.00 NE2 A:HIS183 1.9 44.1 1.0 O A:HOH939 1.9 41.7 1.0 NE2 B:HIS142 2.0 40.6 1.0 OD2 B:ASP185 2.0 38.4 1.0 CG B:ASP185 2.7 34.9 1.0 OD1 B:ASP185 2.9 35.4 1.0 CE1 A:HIS183 2.9 41.1 1.0 CD2 B:HIS142 2.9 44.9 1.0 CE1 B:HIS142 3.0 44.1 1.0 CD2 A:HIS183 3.0 41.4 1.0 OD2 A:ASP180 4.0 47.0 1.0 O B:HOH948 4.0 51.7 1.0 ND1 A:HIS183 4.0 41.0 1.0 O B:HOH990 4.0 40.8 1.0 ND1 B:HIS142 4.1 49.0 1.0 CG B:HIS142 4.1 43.1 1.0 CG A:HIS183 4.1 39.1 1.0 CB B:ASP185 4.2 32.8 1.0 O B:MET140 4.4 39.4 1.0 CA B:GLY39 4.6 37.0 1.0 CG A:ASP180 4.7 42.2 1.0 CB A:ASP180 4.7 41.0 1.0 CL B:CL803 4.9 42.6 1.0

Zinc binding site 4 out of 4 in the Artificial Gtpase-Bse Dimer of Human DYNAMIN1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Artificial Gtpase-Bse Dimer of Human DYNAMIN1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn802 b:67.2 occ:1.00 O B:HOH904 2.0 79.2 1.0 OE2 B:GLU310 2.0 81.2 1.0 CD B:GLU310 2.8 69.6 1.0 OE1 B:GLU310 2.9 68.3 1.0 CG B:GLU310 4.2 65.5 1.0

O.M.Ganichkin, R.Vancraenenbroeck, G.Rosenblum, H.Hofmann, O.Daumke, J.K.Noel. Gtpase-Bse Minimal Human DYNAMIN1 Construct To Be Published.