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Atomistry » Sodium » PDB 5wjo-5x2p » 5wn2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 5wjo-5x2p » 5wn2 » |
Sodium in PDB 5wn2: APE1 Exonuclease Substrate Complex with PhosphoglycolateEnzymatic activity of APE1 Exonuclease Substrate Complex with Phosphoglycolate
All present enzymatic activity of APE1 Exonuclease Substrate Complex with Phosphoglycolate:
4.2.99.18; Protein crystallography data
The structure of APE1 Exonuclease Substrate Complex with Phosphoglycolate, PDB code: 5wn2
was solved by
B.D.Freudenthal,
A.M.Whitaker,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5wn2:
The structure of APE1 Exonuclease Substrate Complex with Phosphoglycolate also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the APE1 Exonuclease Substrate Complex with Phosphoglycolate
(pdb code 5wn2). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the APE1 Exonuclease Substrate Complex with Phosphoglycolate, PDB code: 5wn2: Jump to Sodium binding site number: 1; 2; Sodium binding site 1 out of 2 in 5wn2Go back to Sodium Binding Sites List in 5wn2
Sodium binding site 1 out
of 2 in the APE1 Exonuclease Substrate Complex with Phosphoglycolate
Mono view Stereo pair view
Sodium binding site 2 out of 2 in 5wn2Go back to Sodium Binding Sites List in 5wn2
Sodium binding site 2 out
of 2 in the APE1 Exonuclease Substrate Complex with Phosphoglycolate
Mono view Stereo pair view
Reference:
A.M.Whitaker,
T.S.Flynn,
B.D.Freudenthal.
Molecular Snapshots of APE1 Proofreading Mismatches and Removing Dna Damage. Nat Commun V. 9 399 2018.
Page generated: Tue Dec 15 11:47:46 2020
ISSN: ESSN 2041-1723 PubMed: 29374164 DOI: 10.1038/S41467-017-02175-Y |
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