Zinc in PDB 7ftk: Crystal Structure of Apo Human Cyclic Gmp-Amp Synthase

All present enzymatic activity of Crystal Structure of Apo Human Cyclic Gmp-Amp Synthase:
2.7.7.86;

The structure of Crystal Structure of Apo Human Cyclic Gmp-Amp Synthase, PDB code: 7ftk was solved by L.Leibrock, J.Benz, K.Groebke-Zbinden, M.G.Rudolph, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	60.21 / 2.13
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	50.128, 120.413, 127.506, 90, 90, 90
R / Rfree (%)	21.2 / 27.8

The binding sites of Zinc atom in the Crystal Structure of Apo Human Cyclic Gmp-Amp Synthase (pdb code 7ftk). 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 Apo Human Cyclic Gmp-Amp Synthase, PDB code: 7ftk:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Apo Human Cyclic Gmp-Amp Synthase


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 Apo Human Cyclic Gmp-Amp Synthase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn600 b:53.2 occ:1.00 NE2 A:HIS390 2.0 53.4 1.0 SG A:CYS396 2.2 51.0 1.0 O A:HOH709 2.3 30.4 1.0 SG A:CYS404 2.3 45.7 1.0 CD2 A:HIS390 2.8 44.6 1.0 CE1 A:HIS390 3.2 50.0 1.0 CB A:CYS404 3.2 42.0 1.0 N A:CYS404 3.6 52.4 1.0 CB A:CYS396 3.7 44.6 1.0 CA A:CYS404 3.9 50.4 1.0 N A:CYS397 4.0 69.6 1.0 C A:CYS396 4.0 61.8 1.0 CG A:HIS390 4.1 46.6 1.0 ND1 A:HIS390 4.2 47.1 1.0 CA A:CYS396 4.3 55.0 1.0 CB A:CYS397 4.4 66.0 1.0 NH2 A:ARG406 4.4 39.0 1.0 CA A:CYS397 4.4 68.5 1.0 O A:CYS404 4.4 52.9 1.0 C A:CYS404 4.5 55.4 1.0 O A:CYS396 4.5 63.5 1.0 O A:GLU402 4.7 69.4 1.0 C A:LYS403 4.7 58.7 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Apo Human Cyclic Gmp-Amp Synthase


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 Apo Human Cyclic Gmp-Amp Synthase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn600 b:52.9 occ:1.00 NE2 B:HIS390 2.1 51.6 1.0 SG B:CYS396 2.2 52.7 1.0 SG B:CYS397 2.3 50.3 1.0 SG B:CYS404 2.3 52.1 1.0 CD2 B:HIS390 2.9 46.5 1.0 CB B:CYS404 3.3 52.5 1.0 CE1 B:HIS390 3.3 47.6 1.0 CB B:CYS396 3.6 47.0 1.0 CB B:CYS397 3.6 61.7 1.0 N B:CYS404 3.6 56.9 1.0 N B:CYS397 4.0 66.7 1.0 CA B:CYS404 4.0 58.5 1.0 C B:CYS396 4.0 60.9 1.0 CG B:HIS390 4.1 45.9 1.0 ND1 B:HIS390 4.3 46.3 1.0 CA B:CYS396 4.3 55.0 1.0 CA B:CYS397 4.4 71.3 1.0 O B:CYS396 4.4 66.6 1.0 NH2 B:ARG406 4.4 46.8 1.0 C B:CYS404 4.5 56.3 1.0 O B:GLU402 4.6 66.5 1.0 O B:CYS404 4.7 51.9 1.0 C B:LYS403 4.8 60.4 1.0

K.Groebke-Zbinden, A.Vandemeulebroucke, M.Hilbert, M.G.Rudolph. Crystal Structure of A Human Cyclic Gmp-Amp Synthase Complex To Be Published.