Zinc in PDB 6vff: Dimer of Human Adenosine Deaminase Acting on Dsrna (ADAR2) Mutant E488Q Bound to Dsrna Sequence Derived From Human GLI1 Gene

All present enzymatic activity of Dimer of Human Adenosine Deaminase Acting on Dsrna (ADAR2) Mutant E488Q Bound to Dsrna Sequence Derived From Human GLI1 Gene:
3.5.4.37;

The structure of Dimer of Human Adenosine Deaminase Acting on Dsrna (ADAR2) Mutant E488Q Bound to Dsrna Sequence Derived From Human GLI1 Gene, PDB code: 6vff was solved by A.S.Thuy-Boun, A.J.Fisher, P.A.Beal, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.48 / 2.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	170.000, 63.210, 142.200, 90.00, 118.13, 90.00
R / Rfree (%)	19.7 / 24.8

The binding sites of Zinc atom in the Dimer of Human Adenosine Deaminase Acting on Dsrna (ADAR2) Mutant E488Q Bound to Dsrna Sequence Derived From Human GLI1 Gene (pdb code 6vff). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Dimer of Human Adenosine Deaminase Acting on Dsrna (ADAR2) Mutant E488Q Bound to Dsrna Sequence Derived From Human GLI1 Gene, PDB code: 6vff:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Dimer of Human Adenosine Deaminase Acting on Dsrna (ADAR2) Mutant E488Q Bound to Dsrna Sequence Derived From Human GLI1 Gene


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Dimer of Human Adenosine Deaminase Acting on Dsrna (ADAR2) Mutant E488Q Bound to Dsrna Sequence Derived From Human GLI1 Gene within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn802 b:56.6 occ:1.00 O6 C:8AZ13 2.0 49.6 1.0 ND1 A:HIS394 2.0 52.5 1.0 SG A:CYS451 2.3 60.2 1.0 SG A:CYS516 2.4 52.0 1.0 CE1 A:HIS394 2.9 55.5 1.0 CG A:HIS394 3.0 54.8 1.0 C6 C:8AZ13 3.1 59.2 1.0 CB A:CYS516 3.1 53.5 1.0 C5 C:8AZ13 3.4 58.1 1.0 CB A:HIS394 3.5 53.1 1.0 N1 C:8AZ13 3.5 60.5 1.0 CB A:CYS451 3.5 48.1 1.0 OE2 A:GLU396 3.6 60.8 1.0 CE A:LYS483 3.6 58.9 1.0 C2 C:8AZ13 3.8 57.7 1.0 N A:CYS451 3.8 47.8 1.0 NE2 A:HIS394 4.0 52.9 1.0 C4 C:8AZ13 4.0 59.8 1.0 CD2 A:HIS394 4.1 56.1 1.0 NZ A:LYS483 4.1 55.3 1.0 N7 C:8AZ13 4.1 67.1 1.0 N A:CYS516 4.1 52.3 1.0 CA A:CYS516 4.2 52.5 1.0 N3 C:8AZ13 4.3 57.6 1.0 CA A:CYS451 4.3 49.4 1.0 CD A:GLU396 4.4 59.1 1.0 OE1 A:GLU396 4.7 61.0 1.0 N9 C:8AZ13 4.9 61.4 1.0 CA A:HIS394 4.9 50.0 1.0 N8 C:8AZ13 4.9 70.3 1.0 C A:PRO450 4.9 52.5 1.0 CD A:LYS483 4.9 55.0 1.0

Zinc binding site 2 out of 2 in the Dimer of Human Adenosine Deaminase Acting on Dsrna (ADAR2) Mutant E488Q Bound to Dsrna Sequence Derived From Human GLI1 Gene


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Dimer of Human Adenosine Deaminase Acting on Dsrna (ADAR2) Mutant E488Q Bound to Dsrna Sequence Derived From Human GLI1 Gene within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn802 b:57.0 occ:1.00 O B:HOH901 2.0 55.2 1.0 ND1 B:HIS394 2.1 58.9 1.0 SG B:CYS451 2.2 50.9 1.0 SG B:CYS516 2.2 60.2 1.0 CB B:CYS516 3.0 62.0 1.0 CE1 B:HIS394 3.0 61.8 1.0 CG B:HIS394 3.1 57.7 1.0 CB B:CYS451 3.4 52.8 1.0 CB B:HIS394 3.6 58.3 1.0 CE B:LYS483 3.6 57.2 1.0 N B:CYS451 3.8 58.5 1.0 N B:CYS516 3.9 63.5 1.0 OE2 B:GLU396 4.0 56.3 1.0 CA B:CYS516 4.0 63.5 1.0 NZ B:LYS483 4.1 58.8 1.0 NE2 B:HIS394 4.1 57.7 1.0 CD B:GLU396 4.2 57.4 1.0 CD2 B:HIS394 4.2 59.4 1.0 CA B:CYS451 4.2 58.5 1.0 OE1 B:GLU396 4.3 64.1 1.0 CD B:LYS483 4.9 56.6 1.0 C B:CYS451 5.0 63.6 1.0 CG B:GLU396 5.0 54.8 1.0 O B:CYS451 5.0 63.8 1.0 C B:PRO450 5.0 58.2 1.0 CA B:HIS394 5.0 61.8 1.0

A.S.Thuy-Boun, J.M.Thomas, H.L.Grajo, C.M.Palumbo, S.Park, L.T.Nguyen, A.J.Fisher, P.A.Beal. Asymmetric Dimerization of Adenosine Deaminase Acting on Rna Facilitates Substrate Recognition. Nucleic Acids Res. V. 48 7958 2020.
ISSN: ESSN 1362-4962
PubMed: 32597966
DOI: 10.1093/NAR/GKAA532