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Atomistry » Chlorine » PDB 3zx2-4a7d » 4a2z » |
Chlorine in PDB 4a2z: Crystal Structure of Leishmania Major N-Myristoyltransferase (Nmt) with Bound Myristoyl-Coa and A Pyrazole Sulphonamide LigandEnzymatic activity of Crystal Structure of Leishmania Major N-Myristoyltransferase (Nmt) with Bound Myristoyl-Coa and A Pyrazole Sulphonamide Ligand
All present enzymatic activity of Crystal Structure of Leishmania Major N-Myristoyltransferase (Nmt) with Bound Myristoyl-Coa and A Pyrazole Sulphonamide Ligand:
2.3.1.97; Protein crystallography data
The structure of Crystal Structure of Leishmania Major N-Myristoyltransferase (Nmt) with Bound Myristoyl-Coa and A Pyrazole Sulphonamide Ligand, PDB code: 4a2z
was solved by
D.A.Robinson,
S.Brand,
A.H.Fairlamb,
M.A.J.Ferguson,
J.A.Frearson,
P.G.Wyatt,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Leishmania Major N-Myristoyltransferase (Nmt) with Bound Myristoyl-Coa and A Pyrazole Sulphonamide Ligand
(pdb code 4a2z). 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 Leishmania Major N-Myristoyltransferase (Nmt) with Bound Myristoyl-Coa and A Pyrazole Sulphonamide Ligand, PDB code: 4a2z: Chlorine binding site 1 out of 1 in 4a2zGo back to Chlorine Binding Sites List in 4a2z
Chlorine binding site 1 out
of 1 in the Crystal Structure of Leishmania Major N-Myristoyltransferase (Nmt) with Bound Myristoyl-Coa and A Pyrazole Sulphonamide Ligand
Mono view Stereo pair view
Reference:
S.Brand,
L.A.Cleghorn,
S.P.Mcelroy,
D.A.Robinson,
V.C.Smith,
I.Hallyburton,
J.R.Harrison,
N.R.Norcross,
D.Spinks,
T.Bayliss,
S.Norval,
L.Stojanovski,
L.S.Torrie,
J.A.Frearson,
R.Brenk,
A.H.Fairlamb,
M.A.Ferguson,
K.D.Read,
P.G.Wyatt,
I.H.Gilbert.
Discovery of A Novel Class of Orally Active Trypanocidal N-Myristoyltransferase Inhibitors. J. Med. Chem. V. 55 140 2012.
Page generated: Sat Dec 12 10:22:52 2020
ISSN: ISSN 1520-4804 PubMed: 22148754 DOI: 10.1021/JM201091T |
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