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Zinc in PDB 8e0f: Human Adenosine Deaminase Acting on Dsrna (ADAR2-Rd) Bound to Dsrna Containing A G-G Pair Adjacent to the Target Site

Enzymatic activity of Human Adenosine Deaminase Acting on Dsrna (ADAR2-Rd) Bound to Dsrna Containing A G-G Pair Adjacent to the Target Site

All present enzymatic activity of Human Adenosine Deaminase Acting on Dsrna (ADAR2-Rd) Bound to Dsrna Containing A G-G Pair Adjacent to the Target Site:
3.5.4.37;

Protein crystallography data

The structure of Human Adenosine Deaminase Acting on Dsrna (ADAR2-Rd) Bound to Dsrna Containing A G-G Pair Adjacent to the Target Site, PDB code: 8e0f was solved by X.E.Wilcox, 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) 65.73 / 2.70
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 171.518, 63.389, 142.135, 90, 117.69, 90
R / Rfree (%) 19.3 / 23.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Adenosine Deaminase Acting on Dsrna (ADAR2-Rd) Bound to Dsrna Containing A G-G Pair Adjacent to the Target Site (pdb code 8e0f). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Human Adenosine Deaminase Acting on Dsrna (ADAR2-Rd) Bound to Dsrna Containing A G-G Pair Adjacent to the Target Site, PDB code: 8e0f:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 8e0f

Go back to Zinc Binding Sites List in 8e0f
Zinc binding site 1 out of 2 in the Human Adenosine Deaminase Acting on Dsrna (ADAR2-Rd) Bound to Dsrna Containing A G-G Pair Adjacent to the Target Site


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Adenosine Deaminase Acting on Dsrna (ADAR2-Rd) Bound to Dsrna Containing A G-G Pair Adjacent to the Target Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn802

b:55.0
occ:1.00
O6 C:8AZ13 2.0 60.6 1.0
ND1 A:HIS394 2.0 56.2 1.0
SG A:CYS451 2.3 60.7 1.0
SG A:CYS516 2.4 52.5 1.0
CE1 A:HIS394 2.9 59.1 1.0
CG A:HIS394 3.1 60.6 1.0
C6 C:8AZ13 3.1 66.7 1.0
CB A:CYS516 3.2 55.5 1.0
CB A:CYS451 3.3 58.1 1.0
NZ A:LYS483 3.5 54.0 1.0
CB A:HIS394 3.5 56.7 1.0
C5 C:8AZ13 3.5 63.6 1.0
N1 C:8AZ13 3.6 64.4 1.0
N A:CYS451 3.8 53.1 1.0
OE2 A:GLU396 3.8 60.1 1.0
NE2 A:HIS394 4.0 54.5 1.0
CE A:LYS483 4.1 58.2 1.0
N A:CYS516 4.1 52.0 1.0
C4 C:8AZ13 4.1 62.0 1.0
C2 C:8AZ13 4.1 63.5 1.0
CA A:CYS451 4.1 53.0 1.0
N7 C:8AZ13 4.1 61.6 1.0
CD2 A:HIS394 4.1 59.2 1.0
CA A:CYS516 4.3 53.3 1.0
CD A:GLU396 4.3 60.0 1.0
N3 C:8AZ13 4.4 60.9 1.0
OE1 A:GLU396 4.5 59.6 1.0
N9 C:8AZ13 4.8 60.9 1.0
N8 C:8AZ13 4.9 68.3 1.0
C A:PRO450 4.9 60.4 1.0
CA A:HIS394 5.0 55.5 1.0
C A:CYS451 5.0 52.8 1.0

Zinc binding site 2 out of 2 in 8e0f

Go back to Zinc Binding Sites List in 8e0f
Zinc binding site 2 out of 2 in the Human Adenosine Deaminase Acting on Dsrna (ADAR2-Rd) Bound to Dsrna Containing A G-G Pair Adjacent to the Target Site


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human Adenosine Deaminase Acting on Dsrna (ADAR2-Rd) Bound to Dsrna Containing A G-G Pair Adjacent to the Target Site within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn802

b:62.5
occ:1.00
O B:HOH903 2.0 53.6 1.0
ND1 B:HIS394 2.1 66.5 1.0
SG B:CYS451 2.3 58.0 1.0
SG B:CYS516 2.3 65.2 1.0
CE1 B:HIS394 2.9 62.5 1.0
CB B:CYS516 3.0 61.0 1.0
CG B:HIS394 3.1 59.1 1.0
CB B:CYS451 3.2 60.1 1.0
CE B:LYS483 3.5 60.8 1.0
CB B:HIS394 3.6 58.5 1.0
N B:CYS516 3.8 61.4 1.0
N B:CYS451 3.8 61.5 1.0
OE2 B:GLU396 3.9 55.2 1.0
CA B:CYS516 4.0 58.8 1.0
NE2 B:HIS394 4.0 61.5 1.0
CA B:CYS451 4.1 57.9 1.0
NZ B:LYS483 4.1 59.9 1.0
CD2 B:HIS394 4.2 59.8 1.0
CD B:GLU396 4.3 57.8 1.0
OE1 B:GLU396 4.6 60.9 1.0
O B:CYS451 4.6 67.6 1.0
CD B:LYS483 4.7 61.3 1.0
C B:CYS451 4.7 63.3 1.0

Reference:

E.E.Doherty, A.Karki, X.E.Wilcox, H.G.Mendoza, A.Manjunath, V.J.Matos, A.J.Fisher, P.A.Beal. Adar Activation By Inducing A Syn Conformation at Guanosine Adjacent to An Editing Site. Nucleic Acids Res. V. 50 10857 2022.
ISSN: ESSN 1362-4962
PubMed: 36243986
DOI: 10.1093/NAR/GKAC897
Page generated: Fri Aug 22 09:21:18 2025

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