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Atomistry » Chlorine » PDB 4gen-4glo » 4gf0 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 4gen-4glo » 4gf0 » |
Chlorine in PDB 4gf0: Crystal Structure of Glutahtione Transferase Homolog From Sulfitobacter, Target Efi-501084, with Bound GlutathioneProtein crystallography data
The structure of Crystal Structure of Glutahtione Transferase Homolog From Sulfitobacter, Target Efi-501084, with Bound Glutathione, PDB code: 4gf0
was solved by
M.W.Vetting,
R.Toro,
R.Bhosle,
N.F.Al Obaidi,
L.L.Morisco,
S.R.Wasserman,
S.Sojitra,
E.Washington,
A.Scott Glenn,
S.Chowdhury,
B.Evans,
J.Hammonds,
B.Hillerich,
J.Love,
R.D.Seidel,
H.J.Imker,
R.N.Armstrong,
J.A.Gerlt,
S.C.Almo,
Enzyme Function Initiative (Efi),
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 Glutahtione Transferase Homolog From Sulfitobacter, Target Efi-501084, with Bound Glutathione
(pdb code 4gf0). 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 Glutahtione Transferase Homolog From Sulfitobacter, Target Efi-501084, with Bound Glutathione, PDB code: 4gf0: Chlorine binding site 1 out of 1 in 4gf0Go back to Chlorine Binding Sites List in 4gf0
Chlorine binding site 1 out
of 1 in the Crystal Structure of Glutahtione Transferase Homolog From Sulfitobacter, Target Efi-501084, with Bound Glutathione
Mono view Stereo pair view
Reference:
M.W.Vetting,
R.Toro,
R.Bhosle,
N.F.Al Obaidi,
L.L.Morisco,
S.R.Wasserman,
S.Sojitra,
E.Washington,
A.Scott Glenn,
S.Chowdhury,
B.Evans,
J.Hammonds,
B.Hillerich,
J.Love,
R.D.Seidel,
H.J.Imker,
R.N.Armstrong,
J.A.Gerlt,
S.C.Almo,
Enzyme Function Initiative (Efi).
Crystal Structure of Glutahtione Transferase Homolog From Sulfitobacter, Target Efi-501084, with Bound Glutathione To Be Published.
Page generated: Sat Dec 12 10:39:24 2020
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