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Atomistry » Chlorine » PDB 6vcm-6vkv » 6vi5 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 6vcm-6vkv » 6vi5 » |
Chlorine in PDB 6vi5: Observing A Ring-Cleaving Dioxygenase in Action Through A Crystalline Lens - A Resting State StructureEnzymatic activity of Observing A Ring-Cleaving Dioxygenase in Action Through A Crystalline Lens - A Resting State Structure
All present enzymatic activity of Observing A Ring-Cleaving Dioxygenase in Action Through A Crystalline Lens - A Resting State Structure:
1.13.11.6; Protein crystallography data
The structure of Observing A Ring-Cleaving Dioxygenase in Action Through A Crystalline Lens - A Resting State Structure, PDB code: 6vi5
was solved by
Y.Wang,
F.Liu,
Y.Yang,
A.Liu,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6vi5:
The structure of Observing A Ring-Cleaving Dioxygenase in Action Through A Crystalline Lens - A Resting State Structure also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Observing A Ring-Cleaving Dioxygenase in Action Through A Crystalline Lens - A Resting State Structure
(pdb code 6vi5). 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 Observing A Ring-Cleaving Dioxygenase in Action Through A Crystalline Lens - A Resting State Structure, PDB code: 6vi5: Chlorine binding site 1 out of 1 in 6vi5Go back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Observing A Ring-Cleaving Dioxygenase in Action Through A Crystalline Lens - A Resting State Structure
![]() Mono view ![]() Stereo pair view
Reference:
Y.Wang,
F.Liu,
Y.Yang,
A.Liu.
Probing Extradiol Dioxygenase Mechanism in Nad+ Biosynthesis By Viewing Reaction Cycle Intermediates Proc.Natl.Acad.Sci.Usa 2020.
Page generated: Sat Jul 12 20:56:29 2025
ISSN: ESSN 1091-6490 DOI: 10.1073/PNAS.2005327117 |
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