Zinc in PDB 4ley: Structure of Mouse Cgas Bound to 18 Bp Dna

The structure of Structure of Mouse Cgas Bound to 18 Bp Dna, PDB code: 4ley was solved by P.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.77 / 2.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	78.377, 145.895, 100.963, 90.00, 90.07, 90.00
R / Rfree (%)	16.1 / 19.1

The binding sites of Zinc atom in the Structure of Mouse Cgas Bound to 18 Bp Dna (pdb code 4ley). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Structure of Mouse Cgas Bound to 18 Bp Dna, PDB code: 4ley:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Structure of Mouse Cgas Bound to 18 Bp Dna


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Mouse Cgas Bound to 18 Bp Dna within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:46.0 occ:1.00 NE2 A:HIS378 2.1 41.9 1.0 SG A:CYS385 2.3 34.0 1.0 SG A:CYS392 2.3 44.7 1.0 SG A:CYS384 2.4 51.6 1.0 CD2 A:HIS378 2.9 41.8 1.0 CE1 A:HIS378 3.2 42.7 1.0 CB A:CYS392 3.3 35.1 1.0 CB A:CYS385 3.3 41.5 1.0 N A:CYS392 3.4 41.0 1.0 CB A:CYS384 3.7 26.3 1.0 N A:CYS385 3.7 42.6 1.0 C A:CYS384 3.9 40.1 1.0 CA A:CYS392 3.9 38.7 1.0 CA A:CYS385 4.1 41.2 1.0 CG A:HIS378 4.2 41.1 1.0 ND1 A:HIS378 4.3 42.3 1.0 O A:CYS384 4.3 41.3 1.0 CA A:CYS384 4.3 32.9 1.0 C A:LYS391 4.4 43.5 1.0 O A:ALA390 4.4 49.1 1.0 C A:CYS392 4.6 44.2 1.0 NH1 A:ARG394 4.6 30.3 1.0 CA A:LYS391 4.7 43.1 1.0 O A:CYS392 4.7 46.2 1.0

Zinc binding site 2 out of 4 in the Structure of Mouse Cgas Bound to 18 Bp Dna


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Mouse Cgas Bound to 18 Bp Dna within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn601 b:43.5 occ:1.00 NE2 B:HIS378 2.1 19.7 1.0 SG B:CYS385 2.3 33.9 1.0 SG B:CYS384 2.3 31.7 1.0 SG B:CYS392 2.4 65.6 1.0 CD2 B:HIS378 2.9 23.0 1.0 CE1 B:HIS378 3.2 19.5 1.0 CB B:CYS392 3.2 26.5 1.0 CB B:CYS385 3.4 28.7 1.0 CB B:CYS384 3.6 33.4 1.0 C B:CYS384 3.7 33.1 1.0 N B:CYS385 3.7 32.8 1.0 N B:CYS392 3.8 37.7 1.0 O B:CYS384 4.0 31.3 1.0 CG B:HIS378 4.1 22.3 1.0 CA B:CYS392 4.1 32.8 1.0 CA B:CYS384 4.1 31.4 1.0 CA B:CYS385 4.1 29.5 1.0 ND1 B:HIS378 4.2 18.5 1.0 NH1 B:ARG394 4.2 24.7 1.0 O B:ALA390 4.5 37.0 1.0 C B:LYS391 4.7 41.7 1.0 C B:CYS392 4.8 36.8 1.0 O B:CYS392 4.9 38.9 1.0

Zinc binding site 3 out of 4 in the Structure of Mouse Cgas Bound to 18 Bp Dna


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structure of Mouse Cgas Bound to 18 Bp Dna within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn601 b:42.8 occ:1.00 NE2 C:HIS378 2.1 40.4 1.0 SG C:CYS384 2.3 43.1 1.0 SG C:CYS385 2.3 36.2 1.0 SG C:CYS392 2.4 43.6 1.0 CD2 C:HIS378 2.8 40.0 1.0 CE1 C:HIS378 3.3 38.5 1.0 CB C:CYS392 3.3 35.7 1.0 O C:HOH713 3.4 45.5 1.0 CB C:CYS385 3.6 33.4 1.0 N C:CYS392 3.7 40.2 1.0 CB C:CYS384 3.7 26.0 1.0 C C:CYS384 3.9 28.4 1.0 N C:CYS385 4.0 29.4 1.0 CG C:HIS378 4.0 35.2 1.0 CA C:CYS392 4.1 37.0 1.0 O C:CYS384 4.2 25.8 1.0 ND1 C:HIS378 4.2 35.1 1.0 NH1 C:ARG394 4.3 27.8 1.0 CA C:CYS384 4.3 28.7 1.0 CA C:CYS385 4.4 30.1 1.0 O C:HOH813 4.4 54.8 1.0 C C:LYS391 4.5 46.4 1.0 O C:HOH736 4.6 74.7 1.0 O C:HOH798 4.7 34.4 1.0 O C:HOH768 4.7 52.9 1.0 C C:CYS392 4.8 37.2 1.0 O C:ALA390 4.8 52.0 1.0 CA C:LYS391 4.9 48.9 1.0 O C:CYS392 4.9 36.4 1.0

Zinc binding site 4 out of 4 in the Structure of Mouse Cgas Bound to 18 Bp Dna


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Structure of Mouse Cgas Bound to 18 Bp Dna within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn601 b:46.7 occ:1.00 NE2 D:HIS378 2.0 32.4 1.0 SG D:CYS392 2.4 80.0 1.0 SG D:CYS384 2.4 36.8 1.0 SG D:CYS385 2.4 34.5 1.0 CD2 D:HIS378 2.9 31.0 1.0 CE1 D:HIS378 3.1 32.9 1.0 CB D:CYS392 3.3 39.0 1.0 CB D:CYS385 3.5 35.4 1.0 CB D:CYS384 3.6 34.2 1.0 N D:CYS392 3.7 32.9 1.0 N D:CYS385 3.8 41.0 1.0 C D:CYS384 3.8 38.6 1.0 CG D:HIS378 4.1 30.6 1.0 O D:HOH735 4.1 27.3 1.0 CA D:CYS392 4.1 31.9 1.0 ND1 D:HIS378 4.1 30.6 1.0 O D:CYS384 4.2 36.3 1.0 CA D:CYS384 4.2 35.8 1.0 CA D:CYS385 4.2 36.8 1.0 O D:HOH756 4.2 28.5 1.0 NH1 D:ARG394 4.4 36.9 1.0 O D:ALA390 4.6 32.7 1.0 C D:LYS391 4.7 36.3 1.0 C D:CYS392 4.8 30.1 1.0

X.Li, C.Shu, G.Yi, C.T.Chaton, C.L.Shelton, J.Diao, X.Zuo, C.C.Kao, A.B.Herr, P.Li. Cyclic Gmp-Amp Synthase Is Activated By Double-Stranded Dna-Induced Oligomerization. Immunity V. 39 1019 2013.
ISSN: ISSN 1074-7613
PubMed: 24332030
DOI: 10.1016/J.IMMUNI.2013.10.019