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Atomistry » Chlorine » PDB 3tnn-3txe » 3toa » |
Chlorine in PDB 3toa: Human Mof Crystal Structure with Active Site Lysine Partially AcetylatedEnzymatic activity of Human Mof Crystal Structure with Active Site Lysine Partially Acetylated
All present enzymatic activity of Human Mof Crystal Structure with Active Site Lysine Partially Acetylated:
2.3.1.48; Protein crystallography data
The structure of Human Mof Crystal Structure with Active Site Lysine Partially Acetylated, PDB code: 3toa
was solved by
H.Yuan,
E.C.Ding,
R.Marmorstein,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3toa:
The structure of Human Mof Crystal Structure with Active Site Lysine Partially Acetylated also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Human Mof Crystal Structure with Active Site Lysine Partially Acetylated
(pdb code 3toa). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Human Mof Crystal Structure with Active Site Lysine Partially Acetylated, PDB code: 3toa: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 3toaGo back to Chlorine Binding Sites List in 3toa
Chlorine binding site 1 out
of 2 in the Human Mof Crystal Structure with Active Site Lysine Partially Acetylated
Mono view Stereo pair view
Chlorine binding site 2 out of 2 in 3toaGo back to Chlorine Binding Sites List in 3toa
Chlorine binding site 2 out
of 2 in the Human Mof Crystal Structure with Active Site Lysine Partially Acetylated
Mono view Stereo pair view
Reference:
H.Yuan,
D.Rossetto,
H.Mellert,
W.Dang,
M.Srinivasan,
J.Johnson,
S.Hodawadekar,
E.C.Ding,
K.Speicher,
N.Abshiru,
R.Perry,
J.Wu,
C.Yang,
Y.G.Zheng,
D.W.Speicher,
P.Thibault,
A.Verreault,
F.B.Johnson,
S.L.Berger,
R.Sternglanz,
S.B.Mcmahon,
J.Cote,
R.Marmorstein.
Myst Protein Acetyltransferase Activity Requires Active Site Lysine Autoacetylation. Embo J. V. 31 58 2011.
Page generated: Sat Dec 12 10:12:52 2020
ISSN: ISSN 0261-4189 PubMed: 22020126 DOI: 10.1038/EMBOJ.2011.382 |
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