Zinc in PDB 7fu7: Crystal Structure of Human Cyclic Gmp-Amp Synthase

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

The structure of Crystal Structure of Human Cyclic Gmp-Amp Synthase, PDB code: 7fu7 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)	59.36 / 2.24
Space group	P 21 2 21
Cell size a, b, c (Å), α, β, γ (°)	45.015, 59.359, 162.405, 90, 90, 90
R / Rfree (%)	22.3 / 24.6

The structure of Crystal Structure of Human Cyclic Gmp-Amp Synthase also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Zinc atom in the Crystal Structure of Human Cyclic Gmp-Amp Synthase (pdb code 7fu7). 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 Human Cyclic Gmp-Amp Synthase, PDB code: 7fu7:

Zinc binding site 1 out of 1 in the Crystal Structure of 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 Human Cyclic Gmp-Amp Synthase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:59.6 occ:1.00 NE2 A:HIS390 2.1 59.6 1.0 SG A:CYS397 2.3 65.7 1.0 SG A:CYS396 2.3 64.6 1.0 SG A:CYS404 2.3 63.8 1.0 CD2 A:HIS390 2.8 44.5 1.0 CE1 A:HIS390 3.2 56.6 1.0 CB A:CYS404 3.3 64.8 1.0 CB A:CYS396 3.7 58.8 1.0 CB A:CYS397 3.7 64.1 1.0 N A:CYS404 3.9 87.0 1.0 N A:CYS397 4.0 72.4 1.0 O A:HOH718 4.0 63.2 1.0 C A:CYS396 4.0 75.0 1.0 CG A:HIS390 4.0 50.5 1.0 CA A:CYS404 4.1 77.7 1.0 ND1 A:HIS390 4.2 53.7 1.0 NH1 A:ARG406 4.3 61.6 1.0 O A:CYS396 4.4 68.2 1.0 CA A:CYS397 4.4 78.2 1.0 CA A:CYS396 4.4 68.7 1.0 C A:CYS404 4.5 74.3 1.0 O A:CYS404 4.6 72.5 1.0 O A:GLU402 4.8 90.6 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.