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Atomistry » Chlorine » PDB 3wav-3wnr » 3wfb » |
Chlorine in PDB 3wfb: Reduced Cytochrome C-Dependent Nitric Oxide Reductase (Cnor) From Pseudomonas Aeruginosa in Complex with Antibody FragmentEnzymatic activity of Reduced Cytochrome C-Dependent Nitric Oxide Reductase (Cnor) From Pseudomonas Aeruginosa in Complex with Antibody Fragment
All present enzymatic activity of Reduced Cytochrome C-Dependent Nitric Oxide Reductase (Cnor) From Pseudomonas Aeruginosa in Complex with Antibody Fragment:
1.7.2.5; Protein crystallography data
The structure of Reduced Cytochrome C-Dependent Nitric Oxide Reductase (Cnor) From Pseudomonas Aeruginosa in Complex with Antibody Fragment, PDB code: 3wfb
was solved by
N.Sato,
S.Ishii,
T.Hino,
H.Sugimoto,
Y.Fukumori,
Y.Shiro,
T.Tosha,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3wfb:
The structure of Reduced Cytochrome C-Dependent Nitric Oxide Reductase (Cnor) From Pseudomonas Aeruginosa in Complex with Antibody Fragment also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Reduced Cytochrome C-Dependent Nitric Oxide Reductase (Cnor) From Pseudomonas Aeruginosa in Complex with Antibody Fragment
(pdb code 3wfb). 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 Reduced Cytochrome C-Dependent Nitric Oxide Reductase (Cnor) From Pseudomonas Aeruginosa in Complex with Antibody Fragment, PDB code: 3wfb: Chlorine binding site 1 out of 1 in 3wfbGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Reduced Cytochrome C-Dependent Nitric Oxide Reductase (Cnor) From Pseudomonas Aeruginosa in Complex with Antibody Fragment
![]() Mono view ![]() Stereo pair view
Reference:
N.Sato,
S.Ishii,
H.Sugimoto,
T.Hino,
Y.Fukumori,
Y.Sako,
Y.Shiro,
T.Tosha.
Structures of Reduced and Ligand-Bound Nitric Oxide Reductase Provide Insights Into Functional Differences in Respiratory Enzymes Proteins 2013.
Page generated: Fri Jul 11 11:58:24 2025
ISSN: ESSN 1097-0134 PubMed: 24338896 DOI: 10.1002/PROT.24492 |
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