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Zinc in PDB 6vff: Dimer of Human Adenosine Deaminase Acting on Dsrna (ADAR2) Mutant E488Q Bound to Dsrna Sequence Derived From Human GLI1 GeneEnzymatic activity of 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; Protein crystallography data
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:
Zinc Binding Sites:
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 6vffGo back to Zinc Binding Sites List in 6vff
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
Zinc binding site 2 out of 2 in 6vffGo back to Zinc Binding Sites List in 6vff
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
Reference:
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.
Page generated: Wed Dec 16 13:01:37 2020
ISSN: ESSN 1362-4962 PubMed: 32597966 DOI: 10.1093/NAR/GKAA532 |
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