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Atomistry » Chlorine » PDB 3tno-3txf » 3tob | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 3tno-3txf » 3tob » |
Chlorine in PDB 3tob: Human Mof E350Q Crystal Structure with Active Site Lysine Partially AcetylatedEnzymatic activity of Human Mof E350Q Crystal Structure with Active Site Lysine Partially Acetylated
All present enzymatic activity of Human Mof E350Q Crystal Structure with Active Site Lysine Partially Acetylated:
2.3.1.48; Protein crystallography data
The structure of Human Mof E350Q Crystal Structure with Active Site Lysine Partially Acetylated, PDB code: 3tob
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 3tob:
The structure of Human Mof E350Q 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 E350Q Crystal Structure with Active Site Lysine Partially Acetylated
(pdb code 3tob). 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 Human Mof E350Q Crystal Structure with Active Site Lysine Partially Acetylated, PDB code: 3tob: Chlorine binding site 1 out of 1 in 3tobGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Human Mof E350Q 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: Sun Jul 21 05:27:31 2024
ISSN: ISSN 0261-4189 PubMed: 22020126 DOI: 10.1038/EMBOJ.2011.382 |
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