Zinc in PDB 6sdn: Trypanosoma Cruzi Farnesyl Diphosphate Synthase in Complex with Fragment J82

The structure of Trypanosoma Cruzi Farnesyl Diphosphate Synthase in Complex with Fragment J82, PDB code: 6sdn 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)	42.48 / 1.51
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	58.025, 58.025, 397.697, 90.00, 90.00, 120.00
R / Rfree (%)	16.2 / 19

The binding sites of Zinc atom in the Trypanosoma Cruzi Farnesyl Diphosphate Synthase in Complex with Fragment J82 (pdb code 6sdn). 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 J82, PDB code: 6sdn:
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 J82


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 J82 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:16.8 occ:0.66 O A:HOH525 1.8 35.2 1.0 O A:HOH642 2.0 26.2 1.0 OD1 A:ASP98 2.0 20.9 1.0 OD2 A:ASP102 2.0 19.4 1.0 O A:HOH523 2.2 28.0 1.0 OD2 A:ASP98 2.6 25.6 1.0 CG A:ASP98 2.6 25.0 1.0 CG A:ASP102 3.0 19.4 1.0 OD1 A:ASP102 3.2 18.6 1.0 HE22 A:GLN167 3.7 61.9 1.0 OD2 A:ASP170 4.1 23.4 1.0 HZ2 A:LYS273 4.1 42.1 1.0 CB A:ASP98 4.1 9.8 1.0 HZ1 A:LYS273 4.3 42.1 1.0 OE1 A:GLN167 4.3 22.0 1.0 HG12 A:VAL171 4.4 28.3 0.5 CB A:ASP102 4.4 13.0 1.0 HE2 A:MET101 4.4 19.5 1.0 O A:HOH532 4.4 25.9 1.0 NE2 A:GLN167 4.4 51.6 1.0 HB2 A:ASP98 4.5 11.8 1.0 HA A:ASP98 4.5 10.5 1.0 O A:ASP98 4.6 11.0 1.0 HB2 A:ASP102 4.6 15.6 1.0 NZ A:LYS273 4.6 35.1 1.0 HB3 A:ASP98 4.6 11.8 1.0 HB3 A:ASP102 4.7 15.6 1.0 HG22 A:VAL171 4.8 23.7 0.5 CA A:ASP98 4.8 8.8 1.0 CD A:GLN167 4.8 35.6 1.0 HG23 A:VAL171 5.0 23.7 0.5 C A:ASP98 5.0 10.5 1.0 HG13 A:VAL171 5.0 28.3 0.5

Zinc binding site 2 out of 2 in the Trypanosoma Cruzi Farnesyl Diphosphate Synthase in Complex with Fragment J82


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 J82 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:18.6 occ:0.52 O A:HOH520 1.9 21.3 1.0 OD2 A:ASP250 2.1 23.5 0.6 O A:HOH673 2.1 20.6 0.5 O A:HOH737 2.1 34.9 1.0 O A:HOH557 2.2 29.3 1.0 O A:HOH630 2.3 24.4 1.0 CG A:ASP250 3.1 25.9 0.6 HE22 A:GLN247 3.4 23.6 1.0 HZ1 A:LYS264 3.4 44.2 1.0 HB3 A:ASP250 3.5 22.0 0.4 OD1 A:ASP250 3.6 29.3 0.6 HB2 A:ASP254 3.7 25.5 1.0 O A:HOH673 3.9 14.2 0.5 OD2 A:ASP254 4.1 23.9 1.0 NE2 A:GLN247 4.1 19.7 1.0 O A:HOH558 4.1 27.3 1.0 OD2 A:ASP268 4.1 20.7 1.0 HE21 A:GLN247 4.1 23.6 1.0 NZ A:LYS264 4.3 36.8 1.0 HA A:ASP251 4.3 19.2 1.0 OD1 A:ASP251 4.3 16.0 1.0 O A:ASP250 4.3 19.2 0.4 O A:HOH619 4.4 35.0 1.0 OD1 A:ASP268 4.4 21.2 1.0 O A:ASP250 4.4 18.7 0.6 CB A:ASP250 4.4 17.9 0.6 CB A:ASP250 4.4 18.4 0.4 HZ2 A:LYS264 4.4 44.2 1.0 HB3 A:ASP250 4.5 21.4 0.6 C A:ASP250 4.6 19.2 0.4 CB A:ASP254 4.6 21.2 1.0 HZ3 A:LYS264 4.6 44.2 1.0 C A:ASP250 4.6 19.0 0.6 CG A:ASP254 4.7 19.8 1.0 CG A:ASP268 4.7 22.1 1.0 HB2 A:ASP250 4.8 22.0 0.4 N A:ASP251 4.9 16.8 1.0 HB3 A:ASP254 5.0 25.5 1.0

F.Magari, A.Heine, G.Klebe. Trypanosoma Cruzi Farnesyl Diphosphate Synthase in Complex with Fragment J82 To Be Published.