Zinc in PDB 7ftx: Crystal Structure of Apo Human Cyclic Gmp-Amp Synthase - Hexagonal Form

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

The structure of Crystal Structure of Apo Human Cyclic Gmp-Amp Synthase - Hexagonal Form, PDB code: 7ftx 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)	82.36 / 2.83
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	101.235, 101.235, 240.332, 90, 90, 120
R / Rfree (%)	24.3 / 27.8

The binding sites of Zinc atom in the Crystal Structure of Apo Human Cyclic Gmp-Amp Synthase - Hexagonal Form (pdb code 7ftx). 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 Apo Human Cyclic Gmp-Amp Synthase - Hexagonal Form, PDB code: 7ftx:

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


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 - Hexagonal Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:37.5 occ:1.00 NE2 A:HIS390 2.0 33.8 1.0 SG A:CYS396 2.3 35.7 1.0 SG A:CYS397 2.3 42.2 1.0 SG A:CYS404 2.4 38.4 1.0 CD2 A:HIS390 2.8 32.5 1.0 CE1 A:HIS390 3.2 34.1 1.0 CB A:CYS404 3.3 38.1 1.0 CB A:CYS397 3.4 38.8 1.0 CB A:CYS396 3.6 34.0 1.0 N A:CYS397 3.7 37.1 1.0 C A:CYS396 3.8 35.9 1.0 N A:CYS404 3.9 40.7 1.0 CG A:HIS390 4.0 31.7 1.0 CA A:CYS397 4.1 38.5 1.0 CA A:CYS404 4.2 39.1 1.0 ND1 A:HIS390 4.2 33.3 1.0 CA A:CYS396 4.2 34.4 1.0 O A:CYS396 4.3 35.9 1.0 O A:GLU402 4.3 46.7 1.0 NH2 A:ARG406 4.4 28.7 1.0 C A:CYS404 4.8 38.6 1.0 N A:GLY391 5.0 31.3 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.