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Atomistry » Chlorine » PDB 2bdg-2bl9 » 2bfd | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 2bdg-2bl9 » 2bfd » |
Chlorine in PDB 2bfd: Reactivity Modulation of Human Branched-Chain Alpha-Ketoacid Dehydrogenase By An Internal Molecular SwitchEnzymatic activity of Reactivity Modulation of Human Branched-Chain Alpha-Ketoacid Dehydrogenase By An Internal Molecular Switch
All present enzymatic activity of Reactivity Modulation of Human Branched-Chain Alpha-Ketoacid Dehydrogenase By An Internal Molecular Switch:
1.2.4.4; Protein crystallography data
The structure of Reactivity Modulation of Human Branched-Chain Alpha-Ketoacid Dehydrogenase By An Internal Molecular Switch, PDB code: 2bfd
was solved by
M.Machius,
R.M.Wynn,
J.L.Chuang,
D.R.Tomchick,
C.A.Brautigam,
D.T.Chuang,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2bfd:
The structure of Reactivity Modulation of Human Branched-Chain Alpha-Ketoacid Dehydrogenase By An Internal Molecular Switch also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Reactivity Modulation of Human Branched-Chain Alpha-Ketoacid Dehydrogenase By An Internal Molecular Switch
(pdb code 2bfd). 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 Reactivity Modulation of Human Branched-Chain Alpha-Ketoacid Dehydrogenase By An Internal Molecular Switch, PDB code: 2bfd: Chlorine binding site 1 out of 1 in 2bfdGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Reactivity Modulation of Human Branched-Chain Alpha-Ketoacid Dehydrogenase By An Internal Molecular Switch
![]() Mono view ![]() Stereo pair view
Reference:
M.Machius,
R.M.Wynn,
J.L.Chuang,
J.Li,
R.Kluger,
D.Yu,
D.R.Tomchick,
C.A.Brautigam,
D.T.Chuang.
A Versatile Conformational Switch Regulates Reactivity in Human Branched-Chain Alpha-Ketoacid Dehydrogenase. Structure V. 14 287 2006.
Page generated: Sat Jul 20 05:41:08 2024
ISSN: ISSN 0969-2126 PubMed: 16472748 DOI: 10.1016/J.STR.2005.10.009 |
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