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Atomistry » Chlorine » PDB 5frd-5fz8 » 5fub | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 5frd-5fz8 » 5fub » |
Chlorine in PDB 5fub: Crystal Structure of Zebrafish Protein Arginine Methyltransferase 2 Catalytic Domain with SahEnzymatic activity of Crystal Structure of Zebrafish Protein Arginine Methyltransferase 2 Catalytic Domain with Sah
All present enzymatic activity of Crystal Structure of Zebrafish Protein Arginine Methyltransferase 2 Catalytic Domain with Sah:
2.1.1.125; Protein crystallography data
The structure of Crystal Structure of Zebrafish Protein Arginine Methyltransferase 2 Catalytic Domain with Sah, PDB code: 5fub
was solved by
V.Cura,
N.Troffer-Charlier,
N.Marechal,
L.Bonnefond,
J.Cavarelli,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5fub:
The structure of Crystal Structure of Zebrafish Protein Arginine Methyltransferase 2 Catalytic Domain with Sah also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Zebrafish Protein Arginine Methyltransferase 2 Catalytic Domain with Sah
(pdb code 5fub). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Zebrafish Protein Arginine Methyltransferase 2 Catalytic Domain with Sah, PDB code: 5fub: Chlorine binding site 1 out of 1 in 5fubGo back to Chlorine Binding Sites List in 5fub
Chlorine binding site 1 out
of 1 in the Crystal Structure of Zebrafish Protein Arginine Methyltransferase 2 Catalytic Domain with Sah
Mono view Stereo pair view
Reference:
V.Cura,
N.Marechal,
N.Troffer-Charlier,
J.M.Strub,
M.J.Van Haren,
N.I.Martin,
S.Cianferani,
L.Bonnefond,
J.Cavarelli.
Structural Studies of Protein Arginine Methyltransferase 2 Reveal Its Interactions with Potential Substrates and Inhibitors. Febs J. V. 284 77 2017.
Page generated: Sat Dec 12 11:45:34 2020
ISSN: ISSN 1742-4658 PubMed: 27879050 DOI: 10.1111/FEBS.13953 |
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