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Atomistry » Fluorine » PDB 3gww-3hkw » 3hfj » |
Fluorine in PDB 3hfj: Bacillus Anthracis Nicotinate Mononucleotide Adenylytransferase (Nadd) in Complex with Inhibitor Cid 3289443Protein crystallography data
The structure of Bacillus Anthracis Nicotinate Mononucleotide Adenylytransferase (Nadd) in Complex with Inhibitor Cid 3289443, PDB code: 3hfj
was solved by
H.Zhang,
N.Huang,
Y.Eyobo,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3hfj:
The structure of Bacillus Anthracis Nicotinate Mononucleotide Adenylytransferase (Nadd) in Complex with Inhibitor Cid 3289443 also contains other interesting chemical elements:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Bacillus Anthracis Nicotinate Mononucleotide Adenylytransferase (Nadd) in Complex with Inhibitor Cid 3289443
(pdb code 3hfj). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Bacillus Anthracis Nicotinate Mononucleotide Adenylytransferase (Nadd) in Complex with Inhibitor Cid 3289443, PDB code: 3hfj: Jump to Fluorine binding site number: 1; 2; Fluorine binding site 1 out of 2 in 3hfjGo back to Fluorine Binding Sites List in 3hfj
Fluorine binding site 1 out
of 2 in the Bacillus Anthracis Nicotinate Mononucleotide Adenylytransferase (Nadd) in Complex with Inhibitor Cid 3289443
Mono view Stereo pair view
Fluorine binding site 2 out of 2 in 3hfjGo back to Fluorine Binding Sites List in 3hfj
Fluorine binding site 2 out
of 2 in the Bacillus Anthracis Nicotinate Mononucleotide Adenylytransferase (Nadd) in Complex with Inhibitor Cid 3289443
Mono view Stereo pair view
Reference:
L.Sorci,
Y.Pan,
Y.Eyobo,
I.Rodionova,
N.Huang,
O.Kurnasov,
S.Zhong,
A.D.Mackerell,
H.Zhang,
A.L.Osterman.
Targeting Nad Biosynthesis in Bacterial Pathogens: Structure-Based Development of Inhibitors of Nicotinate Mononucleotide Adenylyltransferase Nadd. Chem.Biol. V. 16 849 2009.
Page generated: Sun Dec 13 11:47:45 2020
ISSN: ISSN 1074-5521 PubMed: 19716475 DOI: 10.1016/J.CHEMBIOL.2009.07.006 |
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