Zinc in PDB 6sdq: Trypanosoma Cruzi Farnesyl Diphosphate Synthase in Complex with Fragment 2M5N

The structure of Trypanosoma Cruzi Farnesyl Diphosphate Synthase in Complex with Fragment 2M5N, PDB code: 6sdq was solved by F.Magari, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.92 / 1.68
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	57.919, 57.919, 398.079, 90.00, 90.00, 120.00
R / Rfree (%)	16.6 / 18.3

The binding sites of Zinc atom in the Trypanosoma Cruzi Farnesyl Diphosphate Synthase in Complex with Fragment 2M5N (pdb code 6sdq). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Trypanosoma Cruzi Farnesyl Diphosphate Synthase in Complex with Fragment 2M5N, PDB code: 6sdq:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Trypanosoma Cruzi Farnesyl Diphosphate Synthase in Complex with Fragment 2M5N


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Trypanosoma Cruzi Farnesyl Diphosphate Synthase in Complex with Fragment 2M5N within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:24.8 occ:0.54 OD2 A:ASP102 2.1 30.9 1.0 OD1 A:ASP98 2.1 27.5 0.6 O A:HOH502 2.3 34.6 1.0 OD2 A:ASP98 2.6 23.0 0.6 CG A:ASP98 2.7 18.5 0.6 CG A:ASP102 3.0 25.1 1.0 OD1 A:ASP102 3.2 27.0 1.0 HB3 A:ASP98 3.2 19.8 0.4 OE1 A:GLN167 3.7 31.0 0.6 HZ1 A:LYS273 3.9 45.8 1.0 OD2 A:ASP170 4.1 28.0 1.0 HE22 A:GLN167 4.1 32.1 0.6 CB A:ASP98 4.2 16.4 0.4 CB A:ASP98 4.2 16.6 0.6 HZ3 A:LYS273 4.2 45.8 1.0 HE3 A:MET101 4.2 35.7 1.0 O A:HOH609 4.4 29.2 1.0 CB A:ASP102 4.4 20.4 1.0 CG A:ASP98 4.5 18.4 0.4 NZ A:LYS273 4.5 38.1 1.0 O A:ASP98 4.5 16.2 0.6 O A:ASP98 4.5 16.1 0.4 HA A:ASP98 4.6 18.1 0.6 HB2 A:ASP102 4.6 24.5 1.0 HB2 A:ASP98 4.6 19.9 0.6 CD A:GLN167 4.6 27.4 0.6 HA A:ASP98 4.6 18.3 0.4 OD2 A:ASP98 4.7 17.4 0.4 HB3 A:ASP102 4.7 24.5 1.0 HB3 A:ASP98 4.7 19.9 0.6 NE2 A:GLN167 4.7 26.8 0.6 HB2 A:ASP98 4.8 19.8 0.4 HZ2 A:LYS273 4.8 45.8 1.0 CA A:ASP98 4.8 15.1 0.6 CA A:ASP98 4.8 15.2 0.4 C A:ASP98 5.0 15.4 0.6 C A:ASP98 5.0 15.5 0.4

Zinc binding site 2 out of 2 in the Trypanosoma Cruzi Farnesyl Diphosphate Synthase in Complex with Fragment 2M5N


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Trypanosoma Cruzi Farnesyl Diphosphate Synthase in Complex with Fragment 2M5N within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn403 b:32.2 occ:0.46 O A:HOH525 2.0 30.7 1.0 O A:HOH551 2.1 35.7 1.0 O A:HOH687 2.5 49.4 1.0 HE22 A:GLN247 3.4 26.0 1.0 HB3 A:ASP250 3.5 35.8 1.0 HB2 A:ASP254 3.6 38.5 1.0 OD1 A:ASP254 3.9 33.4 1.0 O A:HOH608 3.9 33.2 1.0 NE2 A:GLN247 4.1 21.7 1.0 OD2 A:ASP268 4.1 27.9 1.0 HE21 A:GLN247 4.1 26.0 1.0 HA A:ASP251 4.2 28.4 1.0 OD1 A:ASP251 4.3 23.2 1.0 O A:ASP250 4.3 25.6 1.0 OD1 A:ASP268 4.4 28.0 1.0 CB A:ASP254 4.5 32.1 1.0 CB A:ASP250 4.5 29.8 1.0 CG A:ASP254 4.5 31.6 1.0 C A:ASP250 4.6 24.0 1.0 CG A:ASP268 4.7 26.9 1.0 HB2 A:ASP250 4.8 35.8 1.0 HB3 A:ASP254 4.9 38.5 1.0 HZ3 A:LYS207 4.9 39.3 1.0 N A:ASP251 4.9 24.0 1.0

F.Magari, A.Heine, G.Klebe. Trypanosoma Cruzi Farnesyl Diphosphate Synthase in Complex with Fragment 2M5N To Be Published.