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Fluorine in PDB 5uos: Crystal Structure of Cblc (Mmachc) (1-238), A Human B12 Processing Enzyme, Complexed with An Antivitamin B12Protein crystallography data
The structure of Crystal Structure of Cblc (Mmachc) (1-238), A Human B12 Processing Enzyme, Complexed with An Antivitamin B12, PDB code: 5uos
was solved by
A.Shanmuganathan,
A.Karasik,
M.Ruetz,
R.Banerjee,
B.Krautler,
M.Koutmos,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5uos:
The structure of Crystal Structure of Cblc (Mmachc) (1-238), A Human B12 Processing Enzyme, Complexed with An Antivitamin B12 also contains other interesting chemical elements:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Crystal Structure of Cblc (Mmachc) (1-238), A Human B12 Processing Enzyme, Complexed with An Antivitamin B12
(pdb code 5uos). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of Cblc (Mmachc) (1-238), A Human B12 Processing Enzyme, Complexed with An Antivitamin B12, PDB code: 5uos: Jump to Fluorine binding site number: 1; 2; Fluorine binding site 1 out of 2 in 5uosGo back to Fluorine Binding Sites List in 5uos
Fluorine binding site 1 out
of 2 in the Crystal Structure of Cblc (Mmachc) (1-238), A Human B12 Processing Enzyme, Complexed with An Antivitamin B12
Mono view Stereo pair view
Fluorine binding site 2 out of 2 in 5uosGo back to Fluorine Binding Sites List in 5uos
Fluorine binding site 2 out
of 2 in the Crystal Structure of Cblc (Mmachc) (1-238), A Human B12 Processing Enzyme, Complexed with An Antivitamin B12
Mono view Stereo pair view
Reference:
M.Ruetz,
A.Shanmuganathan,
C.Gherasim,
A.Karasik,
R.Salchner,
C.Kieninger,
K.Wurst,
R.Banerjee,
M.Koutmos,
B.Krautler.
Antivitamin B12 Inhibition of the Human B12 -Processing Enzyme Cblc: Crystal Structure of An Inactive Ternary Complex with Glutathione As the Cosubstrate. Angew. Chem. Int. Ed. Engl. V. 56 7387 2017.
Page generated: Sun Dec 13 12:39:32 2020
ISSN: ESSN 1521-3773 PubMed: 28544088 DOI: 10.1002/ANIE.201701583 |
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