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Fluorine in PDB 8coj: Crystal Structure of Human Soluble Adenylyl Cyclase Catalytic Domain in Complex with the Inhibitor Tdi-10228Enzymatic activity of Crystal Structure of Human Soluble Adenylyl Cyclase Catalytic Domain in Complex with the Inhibitor Tdi-10228
All present enzymatic activity of Crystal Structure of Human Soluble Adenylyl Cyclase Catalytic Domain in Complex with the Inhibitor Tdi-10228:
4.6.1.1; Protein crystallography data
The structure of Crystal Structure of Human Soluble Adenylyl Cyclase Catalytic Domain in Complex with the Inhibitor Tdi-10228, PDB code: 8coj
was solved by
C.Steegborn,
M.Fushimi,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 8coj:
The structure of Crystal Structure of Human Soluble Adenylyl Cyclase Catalytic Domain in Complex with the Inhibitor Tdi-10228 also contains other interesting chemical elements:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Crystal Structure of Human Soluble Adenylyl Cyclase Catalytic Domain in Complex with the Inhibitor Tdi-10228
(pdb code 8coj). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Crystal Structure of Human Soluble Adenylyl Cyclase Catalytic Domain in Complex with the Inhibitor Tdi-10228, PDB code: 8coj: Fluorine binding site 1 out of 1 in 8cojGo back to Fluorine Binding Sites List in 8coj
Fluorine binding site 1 out
of 1 in the Crystal Structure of Human Soluble Adenylyl Cyclase Catalytic Domain in Complex with the Inhibitor Tdi-10228
Mono view Stereo pair view
Reference:
S.Sun,
M.Fushimi,
T.Rossetti,
N.Kaur,
J.Ferreira,
M.Miller,
J.Quast,
J.Van Den Heuvel,
C.Steegborn,
L.R.Levin,
J.Buck,
R.W.Myers,
S.Kargman,
N.Liverton,
P.T.Meinke,
D.J.Huggins.
Scaffold Hopping and Optimization of Small Molecule Soluble Adenyl Cyclase Inhibitors Led By Free Energy Perturbation. J.Chem.Inf.Model. 2023.
Page generated: Thu Jul 27 13:49:13 2023
ISSN: ESSN 1549-960X PubMed: 37060320 DOI: 10.1021/ACS.JCIM.2C01577 |
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