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Atomistry » Calcium » PDB 3vyk-3whd » 3wfb » |
Calcium 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:
Calcium Binding Sites:
The binding sites of Calcium 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 Calcium atom.
In total only one binding site of Calcium was determined in the Reduced Cytochrome C-Dependent Nitric Oxide Reductase (Cnor) From Pseudomonas Aeruginosa in Complex with Antibody Fragment, PDB code: 3wfb: Calcium binding site 1 out of 1 in 3wfbGo back to Calcium Binding Sites List in 3wfb
Calcium 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: Sat Jul 13 21:01:13 2024
ISSN: ESSN 1097-0134 PubMed: 24338896 DOI: 10.1002/PROT.24492 |
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