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Zinc in PDB 5vyd: Crystal Structure of Phosphodiesterase Domain of Rhopde Fusion Protein From the Choanoflagellate Salpingoeca RosettaProtein crystallography data
The structure of Crystal Structure of Phosphodiesterase Domain of Rhopde Fusion Protein From the Choanoflagellate Salpingoeca Rosetta, PDB code: 5vyd
was solved by
R.Prem Kumar,
L.B.Lamarche,
D.D.Oprian,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5vyd:
The structure of Crystal Structure of Phosphodiesterase Domain of Rhopde Fusion Protein From the Choanoflagellate Salpingoeca Rosetta also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Phosphodiesterase Domain of Rhopde Fusion Protein From the Choanoflagellate Salpingoeca Rosetta
(pdb code 5vyd). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Phosphodiesterase Domain of Rhopde Fusion Protein From the Choanoflagellate Salpingoeca Rosetta, PDB code: 5vyd: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 5vydGo back to Zinc Binding Sites List in 5vyd
Zinc binding site 1 out
of 2 in the Crystal Structure of Phosphodiesterase Domain of Rhopde Fusion Protein From the Choanoflagellate Salpingoeca Rosetta
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 5vydGo back to Zinc Binding Sites List in 5vyd
Zinc binding site 2 out
of 2 in the Crystal Structure of Phosphodiesterase Domain of Rhopde Fusion Protein From the Choanoflagellate Salpingoeca Rosetta
Mono view Stereo pair view
Reference:
L.B.Lamarche,
R.P.Kumar,
M.M.Trieu,
E.L.Devine,
L.E.Cohen-Abeles,
D.L.Theobald,
D.D.Oprian.
Purification and Characterization of Rhopde, A Retinylidene/Phosphodiesterase Fusion Protein and Potential Optogenetic Tool From the Choanoflagellate Salpingoeca Rosetta. Biochemistry V. 56 5812 2017.
Page generated: Wed Dec 16 11:13:32 2020
ISSN: ISSN 1520-4995 PubMed: 28976747 DOI: 10.1021/ACS.BIOCHEM.7B00519 |
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