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Iron in PDB 5g6b: Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with Two Molecules of 7-((3-Fluorophenethylamino)Ethyl)Quinolin-2-AmineEnzymatic activity of Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with Two Molecules of 7-((3-Fluorophenethylamino)Ethyl)Quinolin-2-Amine
All present enzymatic activity of Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with Two Molecules of 7-((3-Fluorophenethylamino)Ethyl)Quinolin-2-Amine:
1.14.13.165; Protein crystallography data
The structure of Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with Two Molecules of 7-((3-Fluorophenethylamino)Ethyl)Quinolin-2-Amine, PDB code: 5g6b
was solved by
J.K.Holden,
T.L.Poulos,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5g6b:
The structure of Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with Two Molecules of 7-((3-Fluorophenethylamino)Ethyl)Quinolin-2-Amine also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with Two Molecules of 7-((3-Fluorophenethylamino)Ethyl)Quinolin-2-Amine
(pdb code 5g6b). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with Two Molecules of 7-((3-Fluorophenethylamino)Ethyl)Quinolin-2-Amine, PDB code: 5g6b: Iron binding site 1 out of 1 in 5g6bGo back to Iron Binding Sites List in 5g6b
Iron binding site 1 out
of 1 in the Structure of Bacillus Subtilis Nitric Oxide Synthase in Complex with Two Molecules of 7-((3-Fluorophenethylamino)Ethyl)Quinolin-2-Amine
Mono view Stereo pair view
Reference:
J.K.Holden,
M.C.Lewis,
M.A.Cinelli,
Z.Abdullatif,
A.V.Pensa,
R.B.Silverman,
T.L.Poulos.
Targeting Bacterial Nitric Oxide Synthase with Aminoquinoline-Based Inhibitors. Biochemistry V. 55 5587 2016.
Page generated: Sun Dec 13 16:02:09 2020
ISSN: ISSN 1520-4995 PubMed: 27607918 DOI: 10.1021/ACS.BIOCHEM.6B00786 |
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