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Iodine in PDB 5t12: N-Terminal Domain of Enzyme 1 - NitrogenEnzymatic activity of N-Terminal Domain of Enzyme 1 - Nitrogen
All present enzymatic activity of N-Terminal Domain of Enzyme 1 - Nitrogen:
2.7.3.9; Protein crystallography data
The structure of N-Terminal Domain of Enzyme 1 - Nitrogen, PDB code: 5t12
was solved by
A.M.Stanley,
I.Botos,
S.K.Buchanan,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Iodine Binding Sites:
The binding sites of Iodine atom in the N-Terminal Domain of Enzyme 1 - Nitrogen
(pdb code 5t12). This binding sites where shown within
5.0 Angstroms radius around Iodine atom.
In total 5 binding sites of Iodine where determined in the N-Terminal Domain of Enzyme 1 - Nitrogen, PDB code: 5t12: Jump to Iodine binding site number: 1; 2; 3; 4; 5; Iodine binding site 1 out of 5 in 5t12Go back to Iodine Binding Sites List in 5t12
Iodine binding site 1 out
of 5 in the N-Terminal Domain of Enzyme 1 - Nitrogen
Mono view Stereo pair view
Iodine binding site 2 out of 5 in 5t12Go back to Iodine Binding Sites List in 5t12
Iodine binding site 2 out
of 5 in the N-Terminal Domain of Enzyme 1 - Nitrogen
Mono view Stereo pair view
Iodine binding site 3 out of 5 in 5t12Go back to Iodine Binding Sites List in 5t12
Iodine binding site 3 out
of 5 in the N-Terminal Domain of Enzyme 1 - Nitrogen
Mono view Stereo pair view
Iodine binding site 4 out of 5 in 5t12Go back to Iodine Binding Sites List in 5t12
Iodine binding site 4 out
of 5 in the N-Terminal Domain of Enzyme 1 - Nitrogen
Mono view Stereo pair view
Iodine binding site 5 out of 5 in 5t12Go back to Iodine Binding Sites List in 5t12
Iodine binding site 5 out
of 5 in the N-Terminal Domain of Enzyme 1 - Nitrogen
Mono view Stereo pair view
Reference:
M.Strickland,
A.M.Stanley,
G.Wang,
I.Botos,
C.D.Schwieters,
S.K.Buchanan,
A.Peterkofsky,
N.Tjandra.
Structure of the Npr:Ein(Ntr) Complex: Mechanism For Specificity in Paralogous Phosphotransferase Systems. Structure V. 24 2127 2016.
Page generated: Sun Dec 13 19:41:02 2020
ISSN: ISSN 1878-4186 PubMed: 27839951 DOI: 10.1016/J.STR.2016.10.007 |
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