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Atomistry » Calcium » PDB 5fk0-5g38 » 5ful » |
Calcium in PDB 5ful: Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 with SahEnzymatic activity of Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 with Sah
All present enzymatic activity of Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 with Sah:
2.1.1.125; Protein crystallography data
The structure of Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 with Sah, PDB code: 5ful
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 5ful:
The structure of Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 with Sah also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 with Sah
(pdb code 5ful). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 with Sah, PDB code: 5ful: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 5fulGo back to Calcium Binding Sites List in 5ful
Calcium binding site 1 out
of 2 in the Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 with Sah
Mono view Stereo pair view
Calcium binding site 2 out of 2 in 5fulGo back to Calcium Binding Sites List in 5ful
Calcium binding site 2 out
of 2 in the Crystal Structure of Mus Musculus Protein Arginine Methyltransferase 2 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: Sun Jul 14 19:22:53 2024
ISSN: ISSN 1742-4658 PubMed: 27879050 DOI: 10.1111/FEBS.13953 |
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