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Atomistry » Chlorine » PDB 5frd-5fz8 » 5fwd | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 5frd-5fz8 » 5fwd » |
Chlorine in PDB 5fwd: Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 with CP2Enzymatic activity of Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 with CP2
All present enzymatic activity of Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 with CP2:
2.1.1.125; Protein crystallography data
The structure of Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 with CP2, PDB code: 5fwd
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 5fwd:
The structure of Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 with CP2 also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 with CP2
(pdb code 5fwd). 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 Mus Musculus Protein Arginine Methyltransferase 2 with CP2, PDB code: 5fwd: Chlorine binding site 1 out of 1 in 5fwdGo back to Chlorine Binding Sites List in 5fwd
Chlorine binding site 1 out
of 1 in the Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 with CP2
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 11:45:42 2020
ISSN: ISSN 1742-464X PubMed: 27879050 DOI: 10.1111/FEBS.13953 |
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