Zinc in PDB 6edb: Crystal Structure of Sry.Hcgas-21BP Dsdna Complex

All present enzymatic activity of Crystal Structure of Sry.Hcgas-21BP Dsdna Complex:
2.7.7.86;

The structure of Crystal Structure of Sry.Hcgas-21BP Dsdna Complex, PDB code: 6edb was solved by W.Xie, L.Lama, C.Adura, J.F.Glickman, T.Tuschl, D.J.Patel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.01 / 3.21
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	90.307, 115.827, 159.077, 90.00, 90.00, 90.00
R / Rfree (%)	25.5 / 30.2

The binding sites of Zinc atom in the Crystal Structure of Sry.Hcgas-21BP Dsdna Complex (pdb code 6edb). 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 Sry.Hcgas-21BP Dsdna Complex, PDB code: 6edb:

Zinc binding site 1 out of 1 in the Crystal Structure of Sry.Hcgas-21BP Dsdna Complex


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 Sry.Hcgas-21BP Dsdna Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:30.0 occ:1.00 NE2 A:HIS390 2.0 97.1 1.0 SG A:CYS404 2.2 72.2 1.0 SG A:CYS397 2.2 100.0 1.0 SG A:CYS396 2.7 88.7 1.0 CB A:CYS404 2.8 0.3 1.0 CE1 A:HIS390 2.9 90.4 1.0 CD2 A:HIS390 3.1 79.8 1.0 CB A:CYS397 3.2 87.6 1.0 N A:CYS404 3.3 1.0 1.0 CA A:CYS404 3.6 0.5 1.0 N A:CYS397 3.6 83.6 1.0 C A:CYS396 3.7 73.9 1.0 CB A:CYS396 3.8 71.1 1.0 CA A:CYS397 3.9 81.4 1.0 O A:CYS396 4.0 97.1 1.0 ND1 A:HIS390 4.1 74.4 1.0 O A:CYS404 4.1 0.2 1.0 CG A:HIS390 4.2 62.9 1.0 C A:CYS404 4.2 0.3 1.0 CA A:CYS396 4.4 72.5 1.0 NH1 A:ARG406 4.5 80.5 1.0 C A:LYS403 4.5 99.8 1.0 CA A:LYS403 4.9 0.1 1.0 O A:GLU402 4.9 98.9 1.0 CD A:ARG406 5.0 73.6 1.0

W.Xie, L.Lama, C.Adura, D.Tomita, J.F.Glickman, T.Tuschl, D.J.Patel. Human Cgas Catalytic Domain Has An Additional Dna-Binding Interface That Enhances Enzymatic Activity and Liquid-Phase Condensation. Proc.Natl.Acad.Sci.Usa V. 116 11946 2019.
ISSN: ESSN 1091-6490
PubMed: 31142647
DOI: 10.1073/PNAS.1905013116