Zinc in PDB 4km5: X-Ray Crystal Structure of Human Cyclic Gmp-Amp Synthase (Cgas)

The structure of X-Ray Crystal Structure of Human Cyclic Gmp-Amp Synthase (Cgas), PDB code: 4km5 was solved by P.J.Kranzusch, A.S.Y.Lee, J.M.Berger, J.A.Doudna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.45 / 2.50
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	46.454, 162.700, 58.407, 90.00, 90.00, 90.00
R / Rfree (%)	22.5 / 24

The binding sites of Zinc atom in the X-Ray Crystal Structure of Human Cyclic Gmp-Amp Synthase (Cgas) (pdb code 4km5). 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 X-Ray Crystal Structure of Human Cyclic Gmp-Amp Synthase (Cgas), PDB code: 4km5:

Zinc binding site 1 out of 1 in the X-Ray Crystal Structure of Human Cyclic Gmp-Amp Synthase (Cgas)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of X-Ray Crystal Structure of Human Cyclic Gmp-Amp Synthase (Cgas) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:66.9 occ:1.00 NE2 A:HIS390 2.2 62.9 1.0 SG A:CYS404 2.4 54.0 1.0 SG A:CYS397 2.4 52.9 1.0 SG A:CYS396 2.4 51.1 1.0 CD2 A:HIS390 2.7 45.3 1.0 CE1 A:HIS390 3.4 53.4 1.0 CB A:CYS404 3.5 51.8 1.0 CB A:CYS397 3.5 52.3 1.0 CB A:CYS396 3.7 55.2 1.0 O A:HOH709 3.9 56.6 1.0 N A:CYS397 3.9 52.6 1.0 C A:CYS396 3.9 60.2 1.0 N A:CYS404 3.9 54.5 1.0 CG A:HIS390 4.0 53.3 1.0 O A:GLU402 4.1 74.8 1.0 NH1 A:ARG406 4.1 49.4 1.0 O A:CYS396 4.2 49.9 1.0 CA A:CYS404 4.2 67.2 1.0 CA A:CYS397 4.3 64.3 1.0 ND1 A:HIS390 4.3 50.8 1.0 CA A:CYS396 4.3 59.1 1.0 C A:CYS404 4.7 63.1 1.0 N A:GLY391 4.8 53.6 1.0 CA A:GLY391 4.8 55.9 1.0 O A:CYS404 4.9 62.0 1.0

P.J.Kranzusch, A.S.Lee, J.M.Berger, J.A.Doudna. Structure of Human Cgas Reveals A Conserved Family of Second-Messenger Enzymes in Innate Immunity. Cell Rep V. 3 1362 2013.
ISSN: ESSN 2211-1247
PubMed: 23707061
DOI: 10.1016/J.CELREP.2013.05.008